==================== WARNING: ==================== The following items in your input are not valid Swiss-Prot/TrEMBL IDs or ACs and have been ignored: GUN_BURSO HLPA_HAEIN ==================================================== ID GUN2_RALSO STANDARD; PRT; 426 AA. AC P17974; DT 01-NOV-1990 (Rel. 16, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Endoglucanase precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase) DE (Cellulase). GN EGL. OS Ralstonia solanacearum (Pseudomonas solanacearum). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=305; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=AW; RX MEDLINE=92138626; PubMed=1735723; RA Huang J., Schell M.A.; RT "Role of the two-component leader sequence and mature amino acid RT sequences in extracellular export of endoglucanase EGL from RT Pseudomonas solanacearum."; RL J. Bacteriol. 174:1314-1323(1992). RN [2] RP SEQUENCE OF 1-112 FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=89291722; PubMed=2738021; RA Huang J., Sukordhaman M., Schell M.A.; RT "Excretion of the egl gene product of Pseudomonas solanacearum."; RL J. Bacteriol. 171:3767-3774(1989). RN [3] RP PROCESSING. RX MEDLINE=90307678; PubMed=2195024; RA Huang J., Schell M.A.; RT "Evidence that extracellular export of the endoglucanase encoded by RT egl of Pseudomonas solanacearum occurs by a two-step process RT involving a lipoprotein intermediate."; RL J. Biol. Chem. 265:11628-11632(1990). CC -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-glucosidic CC linkages in cellulose, lichenin and cereal beta-D-glucans. CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- SIMILARITY: Belongs to cellulase family A (family 5 of glycosyl CC hydrolases). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84922; AAA61980.1; -. DR PIR; A42649; A42649. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00150; cellulase; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. KW Cellulose degradation; Hydrolase; Glycosidase; Zymogen; Membrane; KW Lipoprotein; Signal; Palmitate. FT SIGNAL 1 19 FT PROPEP 20 45 FT CHAIN 46 426 Endoglucanase. FT LIPID 20 20 N-palmitoyl cysteine. FT LIPID 20 20 S-diacylglycerol cysteine. FT ACT_SITE 249 249 Proton donor (By similarity). FT ACT_SITE 361 361 Nucleophile (By similarity). SQ SEQUENCE 426 AA; 45578 MW; 51E13AD4442CF4A8 CRC64; MRRCMPLVAA SVAALMLAGC GGGDGDPSLS TASVSATDTT TLKPAATSTT SSVWLTLAKD SAAFTVSGTR TVRYGAGSAW VEKSVSGSGR CTSTFFGKDP AAGVAKVCQL LQGTGTLLWR GVSLAGAEFG EGSLPGTYGS NYIYPSADSV TYYKNKGMNL VRLPFRWERL QPTLNQVFDA NELSRLTGFV NAVTATGQTV LLDPHNYARY YGNVIGSSAV PNSAYADFWR RLATQFKSNP RVILGLMNEP NSMPTEQWLS GANAELAAIR SANASNVVFV PGNAWTGAHS WNQNWYGTPN GTVMKGINDP GHNLVFEVHQ YLDGDSSGQS ANCVSATIGA QRLQDFTTWL RSNGYRGFLG EFGAASNDTC NQAVSNMLTF VKNNADVWTG WAWWAGGPWW GGYMYSIEPS NGVDKPQMSV LAPYLK // ID METQ_HAEIN STANDARD; PRT; 273 AA. AC P31728; DT 01-JUL-1993 (Rel. 26, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Probable D-methionine-binding lipoprotein metQ precursor DE (28 kDa outer membrane protein). GN METQ OR HLPA OR HI0620. OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Serotype B; RX MEDLINE=91100034; PubMed=1987077; RA Chanyangam M., Smith A.L., Moseley S.L., Kuehn M., Jenny P.; RT "Contribution of a 28-kilodalton membrane protein to the virulence of RT Haemophilus influenzae."; RL Infect. Immun. 59:600-608(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Rd / KW20 / ATCC 51907; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G., Fitzhugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RX MEDLINE=20137488; PubMed=10675023; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: This protein is a component of a D-methionine CC permease, a binding protein-dependent, ATP-driven transport CC system (By similarity). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor (Probable). CC -!- SIMILARITY: Belongs to the nlpA lipoprotein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59804; AAA24939.1; -. DR EMBL; U32744; AAC22279.1; -. DR PIR; B64082; B64082. DR TIGR; HI0620; -. DR InterPro; IPR004872; Lipoprotein_9. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR004478; YaeC. DR Pfam; PF03180; Lipoprotein_9; 1. DR TIGRFAMs; TIGR00363; TIGR00363; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Transport; Amino-acid transport; Outer membrane; Lipoprotein; Signal; KW Complete proteome; Palmitate. FT SIGNAL 1 20 Probable. FT CHAIN 21 273 Probable D-methionine-binding lipoprotein FT metQ. FT LIPID 21 21 N-palmitoyl cysteine (Probable). FT LIPID 21 21 S-diacylglycerol cysteine (Probable). FT CONFLICT 249 249 I -> V (in Ref. 1). SQ SEQUENCE 273 AA; 29828 MW; 429838A8AC7DD7D7 CRC64; MKLKQLFAIT AIASALVLTG CKEDKKPEAA AAPLKIKVGV MSGPEHQVAE IAAKVAKEKY GLDVQFVEFN DYALPNEAVS KGDLDANAMQ HKPYLDEDAK AKNLNNLVIV GNTFVYPLAG YSKKIKNVNE LQDGAKVVVP NDPTNRGRAL ILLEKQGLIK LKDANNLLST VLDIVENPKK LNITEVDTSV AARALDDVDL AVVNNTYAGQ VGLNAQDDGV FVEDKDSPYV NIIVSRTDNK DSKAVQDFIK SYQTEEVYQE AQKHFKDGVV KGW // ID 17KD_RICPR STANDARD; PRT; 159 AA. AC P16624; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 17 kDa surface antigen precursor. GN OMP OR RP833. OS Rickettsia prowazekii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=782; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Madrid E; RX MEDLINE=89359171; PubMed=2768201; RA Anderson B.E., Tzianabos T.; RT "Comparative sequence analysis of a genus-common rickettsial antigen RT gene."; RL J. Bacteriol. 171:5199-5201(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Madrid E; RX MEDLINE=99039499; PubMed=9823893; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., RA Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., RA Eriksson A.-S., Winkler H.H., Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor (Probable). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28482; AAA26378.1; ALT_SEQ. DR EMBL; AJ235273; CAA15258.1; -. DR PIR; D33971; D33971. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR008816; Rick_17kDa_Anti. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal; Complete proteome; KW Palmitate. FT SIGNAL 1 19 FT CHAIN 20 159 17 kDa surface antigen. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 159 AA; 16672 MW; A33D404B65EEB071 CRC64; MKLLSKIMII ALAASMLQAC NGQSGMNKQG TGTLLGGAGG ALLGSQFGQG KGQLVGVGVG ALLGAVLGGQ IGASMDEQDR RLLELTSQRA LESAPSGSNI EWRNPDNGNH GYVTPNKTYR NSAGQYCREY TQTVIIGGKQ QKTYGNACRQ PDGQWQVVN // ID ACRA_ECOLI STANDARD; PRT; 397 AA. AC P31223; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Acriflavine resistance protein A precursor. GN ACRA OR MTCA OR LIR OR B0463 OR Z0578 OR ECS0516. OS Escherichia coli, and OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562, 83334; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RA Xu J., Bertrand K.P.; RT "Nucleotide sequence of the acrAB operon from Escherichia coli."; RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / W4573; RX MEDLINE=94012493; PubMed=8407802; RA Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.; RT "Molecular cloning and characterization of acrA and acrE genes of RT Escherichia coli."; RL J. Bacteriol. 175:6299-6313(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP SEQUENCE FROM N.A. RA Roberts D., Allen E., Araujo R., Aparicio A., Chung E., Davis K., RA Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., RA Lew H., Lin D., Namath A., Oefner P., Schramm S., Davis R.W.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC STRAIN=O157:H7 / EDL933 / ATCC 700927; RX MEDLINE=21074935; PubMed=11206551; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=O157:H7 / RIMD 0509952; RX MEDLINE=21156231; PubMed=11258796; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). RN [7] RP CHARACTERIZATION. RX MEDLINE=95379493; PubMed=7651136; RA Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., Hearst J.E.; RT "Genes acrA and acrB encode a stress-induced efflux system of RT Escherichia coli."; RL Mol. Microbiol. 16:45-55(1995). RN [8] RP PROCESSING, AND INTERACTION WITH ACRB. RX MEDLINE=20381028; PubMed=10920254; RA Kawabe T., Fujihira E., Yamaguchi A.; RT "Molecular construction of a multidrug exporter system, AcrAB: RT molecular interaction between AcrA and AcrB, and cleavage of the RT N-terminal signal sequence of AcrA."; RL J. Biochem. 128:195-200(2000). CC -!- FUNCTION: AcraB is a drug efflux protein with a broad substrate CC specificity. CC -!- SUBUNIT: Interacts with acrB. CC -!- SUBCELLULAR LOCATION: Attached to the inner membrane by a lipid CC anchor. CC -!- SIMILARITY: Belongs to the acrA/acrE family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M94248; AAA23410.1; -. DR EMBL; U00734; AAA67134.1; -. DR EMBL; AE000152; AAC73565.1; -. DR EMBL; U82664; AAB40217.1; -. DR EMBL; AE005225; AAG54812.1; -. DR EMBL; AP002551; BAB33939.1; -. DR PIR; A36938; A36938. DR PIR; D90693; D90693. DR PIR; H85543; H85543. DR EcoGene; EG11703; acrA. DR InterPro; IPR006143; HlyD. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00529; HlyD; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Transport; Inner membrane; Signal; Antibiotic resistance; Lipoprotein; KW Complete proteome; Palmitate. FT SIGNAL 1 24 FT CHAIN 25 397 Acriflavine resistance protein A. FT LIPID 25 25 N-palmitoyl cysteine (Potential). FT LIPID 25 25 S-diacylglycerol cysteine (Potential). SQ SEQUENCE 397 AA; 42196 MW; 5B81DD5BC2B0A077 CRC64; MNKNRGFTPL AVVLMLSGSL ALTGCDDKQA QQGGQQMPAV GVVTVKTEPL QITTELPGRT SAYRIAEVRP QVSGIILKRN FKEGSDIEAG VSLYQIDPAT YQATYDSAKG DLAKAQAAAN IAQLTVNRYQ KLLGTQYISK QEYDQALADA QQANAAVTAA KAAVETARIN LAYTKVTSPI SGRIGKSNVT EGALVQNGQA TALATVQQLD PIYVDVTQSS NDFLRLKQEL ANGTLKQENG KAKVSLITSD GIKFPQDGTL EFSDVTVDQT TGSITLRAIF PNPDHTLLPG MFVRARLEEG LNPNAILVPQ QGVTRTPRGD ATVLVVGADD KVETRPIVAS QAIGDKWLVT EGLKAGDRVV ISGLQKVRPG VQVKAQEVTA DNNQQAASGA QPEQSKS // ID ANIA_NEIGO STANDARD; PRT; 392 AA. AC Q02219; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Major outer membrane protein Pan 1 precursor. GN ANIA. OS Neisseria gonorrhoeae. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=485; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=R10; RX MEDLINE=93014187; PubMed=1383156; RA Hoehn G.T., Clark V.L.; RT "Isolation and nucleotide sequence of the gene (aniA) encoding the RT major anaerobically induced outer membrane protein of Neisseria RT gonorrhoeae."; RL Infect. Immun. 60:4695-4703(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 33084 / F62; RX MEDLINE=93014188; PubMed=1398981; RA Hoehn G.T., Clark V.L.; RT "The major anaerobically induced outer membrane protein of Neisseria RT gonorrhoeae, Pan 1, is a lipoprotein."; RL Infect. Immun. 60:4704-4708(1992). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor (Probable). CC -!- INDUCTION: By anaerobiosis. CC -!- SIMILARITY: Contains 2 plastocyanin-like domains. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97926; AAA25462.1; -. DR PIR; A49208; A49208. DR PDB; 1KBV; 27-FEB-02. DR PDB; 1KBW; 27-FEB-02. DR InterPro; IPR001117; Cu-oxidase. DR InterPro; IPR001287; CuNO2_reductase. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00394; Cu-oxidase; 2. DR PRINTS; PR00695; CUNO2RDTASE. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Repeat; Outer membrane; Lipoprotein; Signal; 3D-structure; Palmitate. FT SIGNAL 1 18 FT CHAIN 19 392 Major outer membrane protein Pan 1. FT LIPID 19 19 N-palmitoyl cysteine (Probable). FT LIPID 19 19 S-diacylglycerol cysteine (Probable). FT DOMAIN 101 195 Plastocyanin-like 1. FT DOMAIN 245 346 Plastocyanin-like 2. FT DOMAIN 368 387 4 X 5 AA TANDEM REPEATS OF A-A-S-A-P. FT REPEAT 368 372 1. FT REPEAT 373 377 2. FT REPEAT 378 382 3. FT REPEAT 383 387 4. FT STRAND 56 58 FT STRAND 62 62 FT TURN 64 65 FT STRAND 78 93 FT TURN 94 95 FT STRAND 96 103 FT TURN 104 105 FT STRAND 106 106 FT STRAND 111 115 FT TURN 116 117 FT STRAND 119 126 FT TURN 128 129 FT STRAND 134 134 FT STRAND 137 138 FT TURN 139 140 FT HELIX 144 147 FT TURN 148 151 FT STRAND 153 153 FT TURN 155 156 FT STRAND 157 164 FT STRAND 169 174 FT HELIX 180 185 FT TURN 186 187 FT STRAND 189 195 FT TURN 197 198 FT STRAND 205 214 FT STRAND 216 216 FT TURN 220 221 FT STRAND 224 226 FT STRAND 228 228 FT HELIX 230 235 FT TURN 236 236 FT STRAND 240 243 FT TURN 244 245 FT TURN 247 250 FT HELIX 252 254 FT STRAND 256 259 FT TURN 260 261 FT STRAND 262 272 FT STRAND 277 282 FT TURN 283 283 FT STRAND 286 286 FT STRAND 288 290 FT HELIX 291 293 FT STRAND 297 298 FT STRAND 301 301 FT STRAND 303 306 FT TURN 308 309 FT STRAND 310 318 FT STRAND 322 328 FT TURN 331 331 FT HELIX 332 336 FT STRAND 340 346 FT TURN 351 353 SQ SEQUENCE 392 AA; 40954 MW; A4707CC87B923C97 CRC64; MKRQALAAMI ASLFALAACG GEQAAQAPAE TPAASAEAAS SAAQATAETP AGELPVIDAV TTHAPEVPPA IDRDYPAKVR VKMETVEKTM KMDDGVEYRY WTFDGDVPGR MIRVREGDTV EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA TFTAPGRTST FSFKALQPGL YIYHCAVAPV GMHIANGMYG LILVEPKEGL PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY VVFNGHVGSI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN PEIMTQKLSD TAYAGSGAAS APAASAPAAS APAASASEKS VY // ID BLC_ECOLI STANDARD; PRT; 177 AA. AC P39281; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Outer membrane lipoprotein blc precursor. GN BLC OR B4149 OR Z5756 OR ECS5130. OS Escherichia coli, and OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562, 83334; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12 / CS520; RX MEDLINE=96032747; PubMed=7559452; RA Bishop R.E., Penfold S.S., Frost L.S., Hoeltje J.-V., Weiner J.H.; RT "Stationary phase expression of a novel Escherichia coli outer RT membrane lipoprotein and its relationship with mammalian RT apolipoprotein D. Implications for the origin of lipocalins."; RL J. Biol. Chem. 270:23097-23103(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=95334362; PubMed=7610040; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., RA Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the RT region from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=O157:H7 / EDL933 / ATCC 700927; RX MEDLINE=21074935; PubMed=11206551; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=O157:H7 / RIMD 0509952; RX MEDLINE=21156231; PubMed=11258796; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). CC -!- FUNCTION: MAY SERVE A STARVATION RESPONSE FUNCTION IN E.COLI. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- SIMILARITY: Belongs to the lipocalin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U21726; AAC46452.1; -. DR EMBL; U14003; AAA97048.1; -. DR EMBL; AE000487; AAC77109.1; -. DR EMBL; AE005648; AAG59350.1; -. DR EMBL; AP002568; BAB38553.1; -. DR PIR; B86111; B86111. DR PIR; B91270; B91270. DR PIR; I84534; I84534. DR HSSP; P05090; 2APD. DR EcoGene; EG12474; blc. DR InterPro; IPR000566; Lipocln_cytFABP. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS00213; LIPOCALIN; 1. KW Lipocalin; Outer membrane; Lipoprotein; Signal; Complete proteome; KW Palmitate. FT SIGNAL 1 18 Probable. FT CHAIN 19 177 Outer membrane lipoprotein blc. FT LIPID 19 19 N-palmitoyl cysteine (Probable). FT LIPID 19 19 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 177 AA; 19851 MW; BFF9A53A099B0048 CRC64; MRLLPLVAAA TAAFLVVACS SPTPPRGVTV VNNFDAKRYL GTWYEIARFD HRFERGLEKV TATYSLRDDG GLNVINKGYN PDRGMWQQSE GKAYFTGAPT RAALKVSFFG PFYGGYNVIA LDREYRHALV CGPDRDYLWI LSRTPTISDE VKQEMLAVAT REGFDVSKFI WVQQPGS // ID BLC_VIBCH STANDARD; PRT; 171 AA. AC Q08790; O31025; O31027; Q9KML7; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Outer membrane lipoprotein blc precursor (Protein vlp). GN BLC OR VLP OR VLPA OR VCA0317. OS Vibrio cholerae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=666; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Classical 569B / ATCC 25870 / Serotype O1; RX MEDLINE=93293328; PubMed=8514410; RA Franzon V.L., Barker A., Manning P.A.; RT "Nucleotide sequence encoding the mannose-fucose-resistant RT hemagglutinin of Vibrio cholerae O1 and construction of a mutant."; RL Infect. Immun. 61:3032-3037(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Classical 569B / ATCC 25870 / Serotype O1, and RC El Tor O17 / Serotype O1; RA Kaewrakon P., Manning P.A.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=El Tor N16961 / Serotype O1; RX MEDLINE=20406833; PubMed=10952301; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., RA Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D., RA Ermolaeva M.D., Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., RA McDonald L., Utterback T., Fleischmann R.D., Nierman W.C., White O., RA Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., RA Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor (By similarity). CC -!- SIMILARITY: Belongs to the lipocalin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64097; CAA45443.1; -. DR EMBL; AF025662; AAB81982.1; -. DR EMBL; AF025663; AAB81984.1; -. DR EMBL; AE004370; AAF96225.1; -. DR PIR; G82474; G82474. DR PIR; S37731; S37731. DR HSSP; P09464; 1BBP. DR TIGR; VCA0317; -. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR000566; Lipocln_cytFABP. DR Pfam; PF00061; lipocalin; 1. DR PRINTS; PR00179; LIPOCALIN. DR PROSITE; PS00213; LIPOCALIN; 1. KW Lipocalin; Outer membrane; Lipoprotein; Signal; Complete proteome; KW Palmitate. FT SIGNAL 1 15 Probable. FT CHAIN 16 171 Outer membrane lipoprotein blc. FT LIPID 16 16 N-palmitoyl cysteine (Probable). FT LIPID 16 16 S-diacylglycerol cysteine (Probable). FT VARIANT 10 10 S -> A (IN STRAIN N16961). FT VARIANT 68 68 S -> L (IN STRAIN O17). FT CONFLICT 50 50 R -> K (in Ref. 2). FT CONFLICT 170 170 Q -> L (in Ref. 1). SQ SEQUENCE 171 AA; 19686 MW; 447629EE5F9F5306 CRC64; MRAIFLILCS VLLNGCLGMP ESVKPVSDFE LNNYLGKWYE VARLDHSFER GLSQVTAEYR VRNDGGISVL NRGYSEEKGE WKEAEGKAYF VNGSTDGYLK VSFFGPFYGS YVVFELDREN YSYAFVSGPN TEYLWLLSRT PTVERGILDK FIEMSKERGF DTNRLIYVQQ Q // ID BMPA_BORAF STANDARD; PRT; 339 AA. AC O31280; O31281; O31282; O31283; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Basic membrane protein A precursor (Immunodominant antigen P39). GN BMPA. OS Borrelia afzelii. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=29518; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PKO, PWUDI, PLE, and PLJ7; RX MEDLINE=98010210; PubMed=9350727; RA Roessler D., Hauser U., Wilske B.; RT "Heterogeneity of BmpA (P39) among European isolates of Borrelia RT burgdorferi sensu lato and influence of interspecies variability on RT serodiagnosis."; RL J. Clin. Microbiol. 35:2752-2758(1997). CC -!- FUNCTION: Not known; immunogenic protein. CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- SIMILARITY: Belongs to the BMP lipoprotein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X81516; CAA57236.1; -. DR EMBL; X97237; CAA65876.1; -. DR EMBL; X97239; CAA65878.1; -. DR EMBL; X97241; CAA65880.1; -. DR InterPro; IPR003760; Bmp. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF02608; Bmp; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; FALSE_NEG. KW Antigen; Membrane; Lipoprotein; Signal; Palmitate. FT SIGNAL 1 17 Probable. FT CHAIN 18 339 Basic membrane protein A. FT LIPID 18 18 N-palmitoyl cysteine (Probable). FT LIPID 18 18 S-diacylglycerol cysteine (Probable). FT VARIANT 125 125 A -> S (IN STRAIN PLE). FT VARIANT 214 214 I -> T (IN STRAIN PLJ7). FT VARIANT 229 229 A -> P (IN STRAIN PKO). FT VARIANT 254 254 I -> V (IN STRAIN PLJ7). FT VARIANT 268 268 L -> F (IN STRAINS PLE AND PKO). SQ SEQUENCE 339 AA; 36966 MW; 1BEABDF8CBA06FB4 CRC64; MNKILLLILF EGVIFLSCSG KSGLESGIPK VSLVIDGTFD DKSFNESALN GVKKLKEEFE IELVLKESST NSYLSDLEGL KDAGSNLIWL IGYKFSDVAK AVSLQNSEMK YAIIDPVYSN EPIPANLVGM TFRAQEGAFL TGYIAAKVSK TGKIGFLGGI EGDIVDAFRY GYEAGAKYAN KDIKIFSQYI GSFSDLEAGR SVATKMYSDG IDIIHHAAGL GGIGAIEVAK ELGSGHYIIG VDEDQSYLAP NNVITSTTKD VGRSLNLLTS NYLKTNTFEG GKLINYGLKE GVVGFVRNPK MIPFEVEKEI DSLSSKIINK EVIVPYNKES YEKFLKEFI // ID BMPB_BORGA STANDARD; PRT; 341 AA. AC O31362; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Basic membrane protein B precursor. GN BMPB. OS Borrelia garinii. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=29519; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PBI; RX MEDLINE=98010210; PubMed=9350727; RA Roessler D., Hauser U., Wilske B.; RT "Heterogeneity of BmpA (P39) among European isolates of Borrelia RT burgdorferi sensu lato and influence of interspecies variability on RT serodiagnosis."; RL J. Clin. Microbiol. 35:2752-2758(1997). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- SIMILARITY: Belongs to the BMP lipoprotein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X81518; CAA57238.1; -. DR InterPro; IPR003760; Bmp. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF02608; Bmp; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Membrane; Lipoprotein; Signal; Palmitate. FT SIGNAL 1 14 Probable. FT CHAIN 15 341 Basic membrane protein B. FT LIPID 15 15 N-palmitoyl cysteine (Probable). FT LIPID 15 15 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 341 AA; 37236 MW; 442BEF0BFEDD0C9A CRC64; MRIVIFILGI LLTSCFAGNE IESGSSKIKI SMLVDGVLDD KSFNSSANRA LLRLEEDFPE NIEKVFSSAA SGVYSSYVSD LDNLKMNGSD LIWLVGYMLT DASLSVSLEN PKISYGIIDP VYSDDVQIPK NLIGVVFRIE QGAFLAGYIA AKKSVSGKIG FIGGVKGDIV DAFRYGYEAG AKYADKGIEI VSEYSNSFSD VNIGRAIANK MYAKGIDIIH FAAGLAGIGV IEAPKELGDG YYVIGADQDQ SHLAPRNFIT SVIKNVGDAL YLVTSEYLKN NNTWEGGKII QMGLRDGVVG LSNANKFEYI KVIERKIVNE EIIVPYNHEG YEIFIKQILK L // ID BMPC_BORBU STANDARD; PRT; 353 AA. AC O50169; Q44859; Q93V09; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Basic membrane protein C precursor. GN BMPC OR BB0384. OS Borrelia burgdorferi (Lyme disease spirochete). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=139; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=297; RX MEDLINE=95080623; PubMed=7988902; RA Aron L., Alekshun M., Perlee L., Schwartz I., Godfrey H.P., RA Cabello F.; RT "Cloning and DNA sequence analysis of bmpC, a gene encoding a RT potential membrane lipoprotein of Borrelia burgdorferi."; RL FEMS Microbiol. Lett. 123:75-82(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=297; RX MEDLINE=97132632; PubMed=8978084; RA Aron L., Toth C., Godfrey H.P., Cabello F.C.; RT "Identification and mapping of a chromosomal gene cluster of Borrelia RT burgdorferi containing genes expressed in vivo."; RL FEMS Microbiol. Lett. 145:309-314(1996). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BL206; RA Orlova T., Bugrysheva J., Novikova S., Godfrey H.P., Cabello F.C.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 35210 / B31; RX MEDLINE=98065943; PubMed=9403685; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., RA Dougherty B., Tomb J.-F., Fleischmann R.D., Richardson D., RA Peterson J., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J., RA Utterback T., Watthey L., McDonald L., Artiach P., Bowman C., RA Garland S., Fujii C., Cotton M.D., Horst K., Roberts K., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=N40; RX MEDLINE=21065112; PubMed=11136458; RA Dobrikova E.Y., Bugrysheva J., Cabello F.C.; RT "Two independent transcriptional units control the complex and RT simultaneous expression of the bmp paralogous chromosomal gene family RT in Borrelia burgdorferi."; RL Mol. Microbiol. 39:370-378(2001). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- SIMILARITY: Belongs to the BMP lipoprotein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U49938; AAC44711.1; -. DR EMBL; AF400111; AAM89913.1; -. DR EMBL; AE001143; AAC66756.1; -. DR EMBL; AF288609; AAG00583.1; -. DR PIR; G70147; G70147. DR TIGR; BB0384; -. DR InterPro; IPR003760; Bmp. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF02608; Bmp; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 16 Probable. FT CHAIN 17 353 Basic membrane protein C. FT LIPID 17 17 N-palmitoyl cysteine (Probable). FT LIPID 17 17 S-diacylglycerol cysteine (Probable). FT VARIANT 179 179 V -> L (IN STRAIN 297 AND N40). SQ SEQUENCE 353 AA; 39824 MW; 2E8FF607D6CAB9B0 CRC64; MFKRFIFITL SLLVFACFKS NKKSIKSDKV VVGVLAHGSF YDKGYNQSVH DGVVKLRDNF GIKLITKSLR PYPIEGKRLL TVDEAMTEDA YEVQKNPLNL FWLIGYRFSD LSVKLSYERP DIYYGIIDAF DYGDIQVPKN SLAIKFRNEE AAFLAGYIAA KMSRKEKIGF LTGPMSEHVK DFKFGFKAGI FYANPKLRLV SKKAPSLFDK EKGKAMALFM YKEDKVGVIF PIAGITGLGV YDAAKELGPK YYVIGLNQDQ SYIAPQNVIT SIIKDIGKVI YSISSEYINN RVFKGGIIID RGLKEGVIEI VKDPDVLNNR LVDEVIDLEN KIISGEIIVP DSEYAFDLFK SKL // ID BMPD_BORBU STANDARD; PRT; 341 AA. AC Q44743; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Basic membrane protein D precursor. GN BMPD OR BB0385. OS Borrelia burgdorferi (Lyme disease spirochete). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=139; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=JD1; RX MEDLINE=96178617; PubMed=8606088; RA Ramamoorthy R., Povinelli L., Philipp M.T.; RT "Molecular characterization, genomic arrangement, and expression of RT bmpD, a new member of the bmp class of genes encoding membrane RT proteins of Borrelia burgdorferi."; RL Infect. Immun. 64:1259-1264(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 35210 / B31; RX MEDLINE=98065943; PubMed=9403685; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., RA Dougherty B., Tomb J.-F., Fleischmann R.D., Richardson D., RA Peterson J., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J., RA Utterback T., Watthey L., McDonald L., Artiach P., Bowman C., RA Garland S., Fujii C., Cotton M.D., Horst K., Roberts K., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- SIMILARITY: Belongs to the BMP lipoprotein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U35450; AAC43984.1; -. DR EMBL; AE001144; AAB91505.1; -. DR TIGR; BB0385; -. DR InterPro; IPR003760; Bmp. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF02608; Bmp; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 16 Probable. FT CHAIN 17 341 Basic membrane protein D. FT LIPID 17 17 N-palmitoyl cysteine (Probable). FT LIPID 17 17 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 341 AA; 37163 MW; 63FF6638F81A91D5 CRC64; MLKKVYYFLI FLFIVACSSS DDGKSEAKTV SLIVDGAFDD KGFNESSSKA IRKLKADLNI NIIEKASTGN SYLGDIANLE DGNSNLIWGI GFRLSDILFQ RASENVSVNY AIIEGVYDEI QIPKNLLNIS FRSEEVAFLA GYFASKASKT GKIGFVGGVR GKVLESFMYG YEAGAKYANS NIKVVSQYVG TFGDFGLGRS TASNMYRDGV DIIFAAAGLS GIGVIEAAKE LGPDHYIIGV DQDQSYLAPN NVIVSAVKKV DSLMYSLTKK YLETGVLDGG KTMFLGLKED GLGLVLNENL KSNYSEIYNK SLKIGQSIMN GIIKVPYDKV SYDNFVLQME N // ID COML_NEIGO STANDARD; PRT; 267 AA. AC Q50985; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Competence lipoprotein comL precursor. GN COML. OS Neisseria gonorrhoeae. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=485; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=MS11A; RX MEDLINE=96249702; PubMed=8830266; RA Fussenegger M., Facius D., Meier J., Meyer T.F.; RT "A novel peptidoglycan-linked lipoprotein (ComL) that functions in RT natural transformation competence of Neisseria gonorrhoeae."; RL Mol. Microbiol. 19:1095-1105(1996). CC -!- FUNCTION: Required for efficient transformation of Neisseria CC gonorrhoeae by species-related DNA. CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor. CC -!- SIMILARITY: Belongs to the UPF0169 (comL) family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z49895; CAA90076.1; -. DR PIR; S71020; S71020. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR008941; TPR-like. DR InterPro; IPR005156; UPF0169. DR Pfam; PF03696; UPF0169; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Competence; Membrane; Lipoprotein; Signal; Palmitate. FT SIGNAL 1 16 Probable. FT CHAIN 17 267 Competence lipoprotein comL. FT LIPID 17 17 N-palmitoyl cysteine (Probable). FT LIPID 17 17 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 267 AA; 30839 MW; FF4F6BB1A0627EB4 CRC64; MKKILLTVSL GLALSACATQ GTADKDAQIT QDWSVEKLYA EAQDELNSSN YTRAVKLYEI LESRFPTSRH ARQSQLDTAY AYYKDDEKDK ALAAIERFRR LHPQHPNMDY ALYLRGLVLF NEDQSFLNKL ASQDWSDRDP KANREAYQAF AELVQRFPNS KYAADATARM VKLVDALGGN EMSVARYYMK RGAYIAAANR AKKIIGSYQN TRYVEESLAI LELAYKKLDK PQLAADTRRV LETNFPKSPF LTHAWQPDDM PWWRYWH // ID CUTF_ECOLI STANDARD; PRT; 236 AA. AC P40710; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Copper homeostasis protein cutF precursor (Lipoprotein nlpE). GN CUTF OR NLPE OR B0192. OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MC4100; RX MEDLINE=95362642; PubMed=7635808; RA Snyder W.B., Davis L.J., Danese P.N., Cosma C.L., Silhavy T.J.; RT "Overproduction of NlpE, a new outer membrane lipoprotein, suppresses RT the toxicity of periplasmic LacZ by activation of the Cpx signal RT transduction pathway."; RL J. Bacteriol. 177:4216-4223(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MC4100; RX MEDLINE=95362641; PubMed=7635807; RA Gupta S.D., Lee B.T.O., Camakaris J., Wu H.C.; RT "Identification of cutC and cutF (nlpE) genes involved in copper RT tolerance in Escherichia coli."; RL J. Bacteriol. 177:4207-4215(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K12 / W3110; RA Yamamoto Y.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=K12 / W3110; RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the RT 4.0 - 6.0 min (189,987 - 281,416bp) region."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE FROM N.A. RA Schramm S., Duncan M., Allen E., Araujo R., Aparicio A., Chung E., RA Davis K., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., RA Lashkari D., Lew H., Lin D., Namath A., Oefner P., Roberts D., RA Davis R.W.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN COPPER HOMEOSTASIS. COULD BE INVOLVED IN CC BOTH COPPER EFFLUX AND THE DELIVERY OF COPPER TO COPPER-DEPENDENT CC ENZYMES. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18345; AAA86093.1; -. DR EMBL; L38619; AAA82972.1; -. DR EMBL; D49445; BAA08433.1; -. DR EMBL; AE000128; AAC73303.1; -. DR EMBL; D83536; BAA77868.1; -. DR EMBL; U70214; AAB08620.1; -. DR PIR; H64743; H64743. DR EcoGene; EG12137; cutF. DR InterPro; IPR007298; NlpE. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF04170; NlpE; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Copper; Signal; Complete proteome; KW Palmitate. FT SIGNAL 1 20 FT CHAIN 21 236 Copper homeostasis protein cutF. FT LIPID 21 21 N-palmitoyl cysteine. FT LIPID 21 21 S-diacylglycerol cysteine. FT DOMAIN 144 156 COULD CONTAIN A COPPER-BINDING MOTIF. SQ SEQUENCE 236 AA; 25844 MW; 016DAD52EBBE366C CRC64; MVKKAIVTAM AVISLFTLMG CNNRAEVDTL SPAQAAELKP MPQSWRGVLP CADCEGIETS LFLEKDGTWV MNERYLGARE EPSSFASYGT WARTADKLVL TDSKGEKSYY RAKGDALEML DREGNPIESQ FNYTLEAAQS SLPMTPMTLR GMYFYMADAA TFTDCATGKR FMVANNAELE RSYLAARGHS EKPVLLSVEG HFTLEGNPDT GAPTKVLAPD TAGKFYPNQD CSSLGQ // ID CYCR_RHOVI STANDARD; PRT; 356 AA. AC P07173; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Photosynthetic reaction center cytochrome c subunit precursor DE (Cytochrome c558/c559). GN PUFC OR CYTC. OS Rhodopseudomonas viridis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Blastochloris. OX NCBI_TaxID=1079; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE. RC STRAIN=DSM 133; RA Weyer K.A., Lottspeich F., Lang F., Oesterhelt D., Michel H.; RT "Amino acid sequence of the cytochrome subunit of the photosynthetic RT reaction centre from the purple bacterium Rhodopseudomonas viridis."; RL EMBO J. 6:2197-2202(1987). RN [2] RP SEQUENCE OF 1-46 FROM N.A. RA Weyer K.A., Schaefer W., Lottspeich F., Michel H.; RT "The cytochrome subunit of the photosynthetic reaction center from RT Rhodopseudomonas viridis is a lipoprotein."; RL Biochemistry 26:2909-2914(1987). RN [3] RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS). RA Deisenhofer J., Epp O., Miki K., Huber R., Michel H.; RT "Structure of the protein subunits in the photosynthetic reaction RT centre of Rhodopseudomonas viridis at 3-A resolution."; RL Nature 318:618-624(1985). RN [4] RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS). RX MEDLINE=85083091; PubMed=6392571; RA Deisenhofer J., Epp O., Miki K., Huber R., Michel H.; RT "X-ray structure analysis of a membrane protein complex. Electron RT density map at 3-A resolution and a model of the chromophores of the RT photosynthetic reaction center from Rhodopseudomonas viridis."; RL J. Mol. Biol. 180:385-398(1984). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS). RC STRAIN=DSM 133; RX MEDLINE=98035456; PubMed=9351808; RA Lancaster C.R.D., Michel H.; RT "The coupling of light-induced electron transfer and proton uptake as RT derived from crystal structures of reaction centres from RT Rhodopseudomonas viridis modified at the binding site of the RT secondary quinone, QB."; RL Structure 5:1339-1359(1997). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS). RC STRAIN=DSM 133; RX MEDLINE=99150431; PubMed=10024457; RA Lancaster C.R.D., Michel H.; RT "Refined crystal structures of reaction centres from Rhodopseudomonas RT viridis in complexes with the herbicide atrazine and two chiral RT atrazine derivatives also lead to a new model of the bound RT carotenoid."; RL J. Mol. Biol. 286:883-898(1999). CC -!- FUNCTION: The reaction center of purple bacteria contain a tightly CC bound cytochrome molecule which re-reduces the photo oxidized CC primary electron donor. CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor. CC -!- PTM: Binds 4 heme groups per subunit. CC -!- PTM: After the signal sequence is removed, the amino-terminal CC cysteine is modified to form a diacylglyceride thioether, but the CC alpha-amino group is free and is not N-palmitoylated. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05768; CAA29223.1; -. DR EMBL; M16317; AAA26093.1; -. DR PIR; S00139; S00139. DR PDB; 1PRC; 15-OCT-94. DR PDB; 2PRC; 01-APR-99. DR PDB; 3PRC; 01-APR-99. DR PDB; 4PRC; 01-APR-99. DR PDB; 5PRC; 06-APR-99. DR PDB; 6PRC; 06-APR-99. DR PDB; 7PRC; 06-APR-99. DR PDB; 1DXR; 12-JAN-01. DR InterPro; IPR000345; CytC_heme_BS. DR InterPro; IPR003158; CytC_RC. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF02276; CytoC_RC; 1. DR PIRSF; PIRSF000017; RC_cytochrome; 1. DR ProDom; PD010011; CytC_RC; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS00190; CYTOCHROME_C; 4. KW Electron transport; Photosynthesis; Reaction center; Heme; KW Membrane; Lipoprotein; Repeat; Signal; 3D-structure. FT SIGNAL 1 20 FT CHAIN 21 356 Photosynthetic reaction center cytochrome FT c subunit. FT LIPID 21 21 S-diacylglycerol cysteine. FT METAL 94 94 Iron (heme 1 axial ligand). FT BINDING 107 107 Heme 1 (covalent). FT BINDING 110 110 Heme 1 (covalent). FT METAL 111 111 Iron (heme 1 axial ligand). FT METAL 130 130 Iron (heme 2 axial ligand). FT METAL 144 144 Iron (heme 4 axial ligand). FT BINDING 152 152 Heme 2 (covalent). FT BINDING 155 155 Heme 2 (covalent). FT METAL 156 156 Iron (heme 2 axial ligand). FT METAL 253 253 Iron (heme 3 axial ligand). FT BINDING 264 264 Heme 3 (covalent). FT BINDING 267 267 Heme 3 (covalent). FT METAL 268 268 Iron (heme 3 axial ligand). FT BINDING 325 325 Heme 4 (covalent). FT BINDING 328 328 Heme 4 (covalent). FT METAL 329 329 Iron (heme 4 axial ligand). FT STRAND 28 29 FT TURN 35 36 FT STRAND 42 43 FT HELIX 45 55 FT TURN 56 57 FT STRAND 71 71 FT HELIX 72 75 FT TURN 83 84 FT STRAND 86 86 FT HELIX 87 101 FT TURN 103 105 FT HELIX 107 109 FT TURN 110 110 FT STRAND 112 112 FT TURN 113 114 FT STRAND 115 115 FT TURN 116 117 FT HELIX 122 140 FT HELIX 142 145 FT TURN 146 148 FT HELIX 152 156 FT TURN 157 158 FT STRAND 166 166 FT TURN 176 177 FT TURN 182 184 FT TURN 186 187 FT HELIX 189 191 FT HELIX 192 199 FT TURN 200 202 FT HELIX 209 213 FT TURN 214 214 FT STRAND 231 231 FT TURN 232 234 FT HELIX 237 239 FT TURN 243 243 FT HELIX 244 260 FT TURN 261 261 FT HELIX 264 266 FT TURN 267 267 FT STRAND 268 268 FT HELIX 270 272 FT TURN 273 274 FT STRAND 277 277 FT TURN 278 279 FT STRAND 280 280 FT HELIX 282 300 FT TURN 301 302 FT HELIX 303 307 FT TURN 308 308 FT HELIX 311 313 FT TURN 316 317 FT STRAND 322 322 FT HELIX 325 329 FT TURN 330 331 FT HELIX 335 338 FT TURN 342 344 FT HELIX 346 348 SQ SEQUENCE 356 AA; 39371 MW; ECE3D64F1BB0877A CRC64; MKQLIVNSVA TVALASLVAG CFEPPPATTT QTGFRGLSMG EVLHPATVKA KKERDAQYPP ALAAVKAEGP PVSQVYKNVK VLGNLTEAEF LRTMTAITEW VSPQEGCTYC HDENNLASEA KYPYVVARRM LEMTRAINTN WTQHVAQTGV TCYTCHRGTP LPPYVRYLEP TLPLNNRETP THVERVETRS GYVVRLAKYT AYSALNYDPF TMFLANDKRQ VRVVPQTALP LVGVSRGKER RPLSDAYATF ALMMSISDSL GTNCTFCHNA QTFESWGKKS TPQRAIAWWG IRMVRDLNMN YLAPLNASLP ASRLGRQGEA PQADCRTCHQ GVTKPLFGAS RLKDYPELGP IKAAAK // ID GLPQ_HAEIN STANDARD; PRT; 364 AA. AC Q06282; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glycerophosphoryl diester phosphodiesterase precursor (EC 3.1.4.46) DE (Glycerophosphodiester phosphodiesterase) (Surface-exposed lipoprotein DE D) (Protein D) (Immunoglobulin D-binding protein) (IgD-binding DE protein). GN GLPQ OR HPD OR HI0689. OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Rd / KW20 / ATCC 51907; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G., Fitzhugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=NTHI 772; RX MEDLINE=91099948; PubMed=1987023; RA Janson H., Heden L.-O., Grubb A., Ruan M., Forsgren A.; RT "Protein D, an immunoglobulin D-binding protein of Haemophilus RT influenzae: cloning, nucleotide sequence, and expression in RT Escherichia coli."; RL Infect. Immun. 59:119-125(1991). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Minna / Serotype B; RX MEDLINE=94011360; PubMed=8104899; RA Janson H., Ruan M., Forsgren A.; RT "Limited diversity of the protein D gene (hpd) among encapsulated and RT nonencapsulated Haemophilus influenzae strains."; RL Infect. Immun. 61:4546-4552(1993). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=Eagan / Serotype B, 3639, 3640, NCTC 8468 / Serotype B, 6-7626, RC and HK695 / Serotype B; RX MEDLINE=95122210; PubMed=7822043; RA Song X.-M., Forsgren A., Janson H.; RT "The gene encoding protein D (hpd) is highly conserved among RT Haemophilus influenzae type b and nontypeable strains."; RL Infect. Immun. 63:696-699(1995). RN [5] RP CHARACTERIZATION. RC STRAIN=NTHI 772; RX MEDLINE=92192801; PubMed=1548059; RA Janson H., Heden L.-O., Forsgren A.; RT "Protein D, the immunoglobulin D-binding protein of Haemophilus RT influenzae, is a lipoprotein."; RL Infect. Immun. 60:1336-1342(1992). CC -!- FUNCTION: GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE HYDROLYZES CC DEACYLATED PHOSPHOLIPIDS TO G3P AND THE CORRESPONDING ALCOHOLS. CC HAS A SPECIFIC AFFINITY FOR HUMAN IMMUNOGLOBULIN D MYELOMA CC PROTEIN. CC -!- CATALYTIC ACTIVITY: A glycerophosphodiester + H(2)O = an alcohol + CC sn-glycerol 3-phosphate. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- PTM: Contains both ester- and amide-linked fatty acids. CC -!- MISCELLANEOUS: THE SEQUENCE SHOWN IS THAT OF STRAINS NTHI 772 AND CC RD / KW20. CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester CC phosphodiesterase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U32751; AAC22348.1; -. DR EMBL; M37487; AAA24998.1; -. DR EMBL; L12445; AAA24999.1; -. DR EMBL; Z35656; CAA84715.1; -. DR EMBL; Z35657; CAA84716.1; -. DR EMBL; Z35658; CAA84717.1; -. DR EMBL; Z35659; CAA84718.1; -. DR EMBL; Z35660; CAA84719.1; -. DR EMBL; Z35661; CAA84720.1; -. DR PIR; G64086; G64086. DR PIR; S59934; S59934. DR TIGR; HI0689; -. DR InterPro; IPR004129; GDPD. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF03009; GDPD; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Glycerol metabolism; Hydrolase; Signal; Lipoprotein; Outer membrane; KW Complete proteome; Palmitate. FT SIGNAL 1 18 FT CHAIN 19 364 Glycerophosphoryl diester FT phosphodiesterase. FT LIPID 19 19 N-palmitoyl cysteine. FT LIPID 19 19 S-diacylglycerol cysteine. FT VARIANT 13 13 A -> T (IN STRAIN NCTC 8468). FT VARIANT 16 16 L -> V (IN STRAIN NCTC 8468). FT VARIANT 25 25 N -> S (IN STRAIN NCTC 8468). FT VARIANT 28 28 N -> K (IN STRAIN 6-7626). FT VARIANT 34 34 D -> H (IN STRAIN NCTC 8468). FT VARIANT 62 62 H -> Q (IN STRAINS EAGAN; 3639; 3640; FT 6-7626; HK695; MINNA). FT VARIANT 63 63 S -> A (IN STRAINS EAGAN; 3639; 3640; FT NCTC 8468; 6-7626; HK695; MINNA). FT VARIANT 98 98 Y -> H (IN STRAINS EAGAN; 3639; 3640; FT NCTC 8468; 6-7626; HK695; MINNA). FT VARIANT 99 99 R -> H (IN STRAIN NCTC 8468). FT VARIANT 144 144 K -> Q (IN STRAIN 6-7626). FT VARIANT 168 168 K -> R (IN STRAIN 6-7626). FT VARIANT 191 191 T -> A (IN STRAINS EAGAN; 3639; 3640; FT NCTC 8468; 6-7626; HK695; MINNA). FT VARIANT 253 253 P -> S (IN STRAIN 6-7626). FT VARIANT 310 310 Q -> K (IN STRAIN 6-7626). FT VARIANT 327 327 E -> A (IN STRAINS EAGAN; 3639; NCTC FT 8468; 6-7626; HK695; MINNA). FT VARIANT 338 338 A -> V (IN STRAINS EAGAN; 3640; HK695; FT MINNA). FT VARIANT 364 364 K -> E (IN STRAIN 6-7626). SQ SEQUENCE 364 AA; 41902 MW; A6079B3ABF70E820 CRC64; MKLKTLALSL LAAGVLAGCS SHSSNMANTQ MKSDKIIIAH RGASGYLPEH TLESKALAFA QHSDYLEQDL AMTKDGRLVV IHDHFLDGLT DVAKKFPYRH RKDGRYYVID FTLKEIQSLE MTENFETKDG KQAQVYPNRF PLWKSHFRIH TFEDEIEFIQ GLEKSTGKKV GIYPEIKAPW FHHQNGKDIA TETLKVLKKY GYDKKTDMVY LQTFDFNELK RIKTELLPQM GMDLKLVQLI AYTDWKETQE KDPKGYWVNY NYDWMFKPGA MAEVVKYADG VGPGWYMLVN KEESKPDNIV YTPLVKELAQ YNVEVHPYTV RKDALPEFFT DVNQMYDALL NKSGATGVFT DFPDTGVEFL KGIK // ID H8_NEIMC STANDARD; PRT; 183 AA. AC P07212; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE H.8 outer membrane protein precursor. OS Neisseria meningitidis (serogroup C). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=135720; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 700532 / FAM18 / Serogroup C; RX MEDLINE=88216161; PubMed=2452958; RA Kawula T.H., Spinola S.M., Klapper D.G., Cannon J.G.; RT "Localization of a conserved epitope and an azurin-like domain in the RT H.8 protein of pathogenic Neisseria."; RL Mol. Microbiol. 1:179-185(1987). CC -!- COFACTOR: Binds 1 copper ion per molecule (By similarity). CC -!- SIMILARITY: Contains 1 plastocyanin-like domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00530; CAA68589.1; -. DR PIR; S03752; AZNHM. DR HSSP; P00282; 1AZU. DR InterPro; IPR003246; Azurin. DR InterPro; IPR000923; BlueCu_1. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00127; copper-bind; 1. DR ProDom; PD003655; Azurin; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS00196; COPPER_BLUE; 1. KW Lipoprotein; Outer membrane; Copper; Electron transport; Signal; KW Palmitate. FT SIGNAL 1 17 FT CHAIN 18 183 H.8 outer membrane protein. FT LIPID 18 18 N-palmitoyl cysteine. FT LIPID 18 18 S-diacylglycerol cysteine. FT DOMAIN 57 183 Plastocyanin-like. FT METAL 102 102 Copper (By similarity). FT METAL 166 166 Copper (By similarity). FT METAL 171 171 Copper (By similarity). FT METAL 175 175 Copper (By similarity). SQ SEQUENCE 183 AA; 18546 MW; 3F2ECD8910521357 CRC64; MKAYLALISA AVIGLAACSQ EPAAPAAEAT PAAEAPASEA PAAEAAPADA AEAPAAGNCA ATVESNDNMQ FNTKDIQVSK ACKEFTITLK HTGTQPKASM GHNLVIAKAE DMDGVFKDGV GAADTDYVKP DDARVVAHTK LIGGGEESSL TLDPAKLADG DYKFACTFPG HGALMNGKVT LVD // ID HBPA_HAEIN STANDARD; PRT; 547 AA. AC P33950; DT 01-FEB-1994 (Rel. 28, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Heme-binding protein A precursor (Hemin-binding lipoprotein). GN HBPA OR DPPA OR HI0853. OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=DL42 / Serotype B; RX MEDLINE=92267636; PubMed=1339409; RA Hanson M.S., Slaughter C., Hansen E.J.; RT "The hbpA gene of Haemophilus influenzae type b encodes a RT heme-binding lipoprotein conserved among heme-dependent Haemophilus RT species."; RL Infect. Immun. 60:2257-2266(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Rd / KW20 / ATCC 51907; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G., Fitzhugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP POSSIBLE FUNCTION, AND SUBCELLULAR LOCATION. RC STRAIN=DL42 / Serotype B; RX MEDLINE=91251755; PubMed=2041470; RA Hanson M.S., Hansen E.J.; RT "Molecular cloning, partial purification, and characterization of a RT haemin-binding lipoprotein from Haemophilus influenzae type b."; RL Mol. Microbiol. 5:267-278(1991). CC -!- FUNCTION: IMPORTANT ROLE IN HEME ACQUISITION OR METABOLISM. CC -!- SUBCELLULAR LOCATION: Attached to the inner membrane by a lipid CC anchor. CC -!- SIMILARITY: Belongs to the bacterial extracellular solute-binding CC protein family 5. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M88134; AAA73214.1; ALT_SEQ. DR EMBL; M84028; AAA24962.1; -. DR EMBL; U32767; AAC22512.1; ALT_INIT. DR PIR; T45066; T45066. DR HSSP; P23847; 1DPE. DR TIGR; HI0853; -. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR000914; SBP_bac_5. DR Pfam; PF00496; SBP_bac_5; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS01040; SBP_BACTERIAL_5; 1. KW Inner membrane; Signal; Lipoprotein; Complete proteome; Palmitate. FT SIGNAL 1 18 Probable. FT CHAIN 19 547 Heme-binding protein A. FT LIPID 19 19 N-palmitoyl cysteine (Probable). FT LIPID 19 19 S-diacylglycerol cysteine (Probable). FT VARIANT 48 49 KA -> NS (IN STRAIN DL42). FT VARIANT 181 181 T -> N (IN STRAIN DL42). FT VARIANT 240 240 H -> N (IN STRAIN DL42). FT VARIANT 343 343 T -> I (IN STRAIN DL42). FT VARIANT 375 375 A -> V (IN STRAIN DL42). SQ SEQUENCE 547 AA; 60660 MW; 7755E2164A40CB31 CRC64; MKLKATLTLA AATLVLAACD QSSSANKSTA QTEAKSSSNN TFVYCTAKAP LGFSPALIIE GTSYNASSQQ VYNRLVEFKK GSTDIEPALA ESWEISDDGL SYTFHLRKGV KFHTTKEFTP TRDFNADDVV FSFQRQLDPN HPYHNVSKGT YPYFKAMKFP ELLKSVEKVD DNTIRITLNK TDATFLASLG MDFISIYSAE YADSMLKAGK PETLDSRPVG TGPFVFVDYK TDQAIQYVAH ENYWKGRTPL DRLVISIVPD ATTRYAKLQA GTCDLILFPN VADLAKMKTD PKVQLLEQKG LNVAYIAFNT EKAPFDNVKV RQALNYAVDK KAIIEAVYQG AGTSAKNPLP PTIWSYNDEI QDYPYDPEKA KQLLAEAGYP NGFETDFWIQ PVIRASNPNP KRMAELIMAD WAKIGVKTNP VTYEWADYRK RAKEGELTAG IFGWSGDNGD PDNFLSPLLG SSNIGNSNMA RFNNSEFDAL LNEAIGLTNK EERAKLYKQA QVIVHNQAPW IPVAHSVGFA PLSPRVKGYV QSPFGYDAFY GVSVDGK // ID HFD1_HAEIN STANDARD; PRT; 216 AA. AC P45992; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Minor fimbrial subunit hifD precursor. GN HIFD. OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Eagan / Serotype B; RX MEDLINE=95012708; PubMed=7927773; RA McCrea K.W., Watson W.J., Gilsdorf J.R., Marrs C.F.; RT "Identification of hifD and hifE in the pilus gene cluster of RT Haemophilus influenzae type b strain Eagan."; RL Infect. Immun. 62:4922-4928(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=AM30 (770235) / Serotype B; RX MEDLINE=95089703; PubMed=7997179; RA van Ham M.S., van Alphen L., Mooi F.R., van Putten J.P.M.; RT "The fimbrial gene cluster of Haemophilus influenzae type b."; RL Mol. Microbiol. 13:673-684(1994). CC -!- FUNCTION: May be a minor structural protein required for pilus CC biogenesis. CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- SIMILARITY: BELONGS TO THE FIMA/PAPA FAMILY OF FIMBRIA PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13254; AAA61541.1; -. DR EMBL; Z33502; CAA83903.1; -. DR PIR; S54430; S54430. DR InterPro; IPR008966; Adhes_bact. DR InterPro; IPR000259; Fimbrial. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00419; Fimbrial; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Fimbria; Signal; Lipoprotein; Palmitate. FT SIGNAL 1 19 Probable. FT CHAIN 20 216 Minor fimbrial subunit hifD. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 216 AA; 22582 MW; 6DED4B763F395F68 CRC64; MQKTPKKLTA LCHQQSTASC SGSNYSGSNY SGSKCFRLHR LALLACIVAL PAYAVDGRVT FQGEIVSDGT CKIETDSKNR TVTLPTVGKA NLSLAGQTAA PVPFSITLKE CNAADAKKAN LLFSGAVTKG QLYLSNAASS GKANNVGIQI VKADGTGSPI NVDGSQANSE KAPDTGKEQN STVIQPRFDY FAHYYATGAA TAGEVEATAT FQVQYN // ID LOLB_ECOLI STANDARD; PRT; 207 AA. AC P24208; Q46753; DT 01-MAR-1992 (Rel. 21, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Outer-membrane lipoprotein lolB precursor. GN LOLB OR HEMM OR B1209 OR Z1980 OR ECS1714 OR SF1212 OR S1296. OS Escherichia coli, OS Escherichia coli O157:H7, and OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562, 83334, 623; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; RX MEDLINE=93051347; PubMed=1427085; RA Ikemi M., Murakami K., Hashimoto M., Murooka Y.; RT "Cloning and characterization of genes involved in the biosynthesis RT of delta-aminolevulinic acid in Escherichia coli."; RL Gene 121:127-132(1992). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12; RX MEDLINE=93171869; PubMed=7679718; RA Post D.A., Hove-Jensen B., Switzer R.L.; RT "Characterization of the hemA-prs region of the Escherichia coli and RT Salmonella typhimurium chromosomes: identification of two open RT reading frames and implications for prs expression."; RL J. Gen. Microbiol. 139:259-266(1993). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; RA Remler P., Woisetschlaeger M., Strohmaier H.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12; RX MEDLINE=97061202; PubMed=8905232; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., RA Yano M., Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O157:H7 / EDL933 / ATCC 700927; RX MEDLINE=21074935; PubMed=11206551; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O157:H7 / RIMD 0509952; RX MEDLINE=21156231; PubMed=11258796; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [9] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=2457T / ATCC 700930 / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). RN [10] RP CHARACTERIZATION, AND PARTIAL SEQUENCE. RC SPECIES=E.coli; RX MEDLINE=98046025; PubMed=9384574; RA Matsuyama S.-I., Yokota N., Tokuda H.; RT "A novel outer membrane lipoprotein, LolB (HemM), involved in the RT LolA (p20)-dependent localization of lipoproteins to the outer RT membrane of Escherichia coli."; RL EMBO J. 16:6947-6955(1997). CC -!- FUNCTION: Plays a critical role in the incorporation of CC lipoproteins in the outer membrane after they are released by the CC lolA protein. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- SIMILARITY: Belongs to the lolB family. CC -!- CAUTION: Was originally (Ref.1) thought to be involved in delta- CC aminolevulinic acid biosynthesis. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77237; AAA24433.1; -. DR EMBL; D10264; BAA01105.1; -. DR EMBL; U18555; AAC43435.1; -. DR EMBL; AE000219; AAC74293.1; -. DR EMBL; D90756; BAA36067.1; -. DR EMBL; AE005338; AAG56067.1; -. DR EMBL; AP002556; BAB35137.1; -. DR EMBL; AE015148; AAN42825.1; -. DR EMBL; AE016982; AAP16711.1; -. DR PIR; A47706; A47706. DR PIR; B90843; B90843. DR PIR; G85700; G85700. DR PDB; 1IWN; 15-JUL-03. DR EcoGene; EG11293; lolB. DR HAMAP; MF_00233; -; 1. DR InterPro; IPR004565; LolB. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF03550; LolB; 1. DR TIGRFAMs; TIGR00548; lolB; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Chaperone; Outer membrane; Lipoprotein; Transport; Protein transport; KW Signal; Complete proteome; Palmitate; 3D-structure. FT SIGNAL 1 21 FT CHAIN 22 207 Outer-membrane lipoprotein lolB. FT LIPID 22 22 N-palmitoyl cysteine. FT LIPID 22 22 S-diacylglycerol cysteine. FT CONFLICT 12 12 L -> V (in Ref. 1). FT CONFLICT 41 42 QH -> HD (in Ref. 3). FT CONFLICT 176 207 YDTKTQPAMPANMELTDGGQRIKLKMDNWIVK -> MTPKR FT NLRCQPIWNSPTVVNASS (in Ref. 3). SQ SEQUENCE 207 AA; 23551 MW; C517F6E7353B8551 CRC64; MPLPDFRLIR LLPLAALVLT ACSVTTPKGP GKSPDSPQWR QHQQDVRNLN QYQTRGAFAY ISDQQKVYAR FFWQQTGQDR YRLLLTNPLG STELELNAQP GNVQLVDNKG QRYTADDAEE MIGKLTGMPI PLNSLRQWIL GLPGDATDYK LDDQYRLSEI TYSQNGKNWK VVYGGYDTKT QPAMPANMEL TDGGQRIKLK MDNWIVK // ID LP20_HELPY STANDARD; PRT; 175 AA. AC P53436; DT 01-OCT-1996 (Rel. 34, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE LPP20 lipoprotein precursor. GN LPP20 OR HP1456 OR JHP1349. OS Helicobacter pylori (Campylobacter pylori), and OS Helicobacter pylori J99 (Campylobacter pylori J99). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210, 85963; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 40-71 AND 109-134. RC STRAIN=CCUG 17874 / NCTC 11638; RX MEDLINE=95014026; PubMed=7928954; RA Kostrzynska M., O'Toole P.W., Taylor D.E., Trust T.J.; RT "Molecular characterization of a conserved 20-kilodalton membrane- RT associated lipoprotein antigen of Helicobacter pylori."; RL J. Bacteriol. 176:5938-5948(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=26695 / ATCC 700392; RX MEDLINE=97394467; PubMed=9252185; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S., Dougherty B.A., RA Nelson K., Quackenbush J., Zhou L., Kirkness E.F., Peterson S., RA Loftus B., Richardson D., Dodson R., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., RA Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., RA Cotton M.D., Weidman J.M., Fujii C., Bowman C., Watthey L., Wallin E., RA Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., RA Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=J99; RX MEDLINE=99120557; PubMed=9923682; RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., RA Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., RA Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., RA Trust T.J.; RT "Genomic sequence comparison of two unrelated isolates of the human RT gastric pathogen Helicobacter pylori."; RL Nature 397:176-180(1999). CC -!- FUNCTION: COULD PLAY A ROLE IN THE PATHOGENESIS OF H.PYLORI CC DISEASE BY SERVING AS AN INFLAMMATORY MEDIATOR. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor (Probable). CC -!- PTM: The N-terminus is blocked. CC -!- MASS SPECTROMETRY: MW=18283; MW_ERR=150; METHOD=MALDI. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U12429; AAA50860.1; -. DR EMBL; AE000645; AAD08494.1; -. DR EMBL; AE001557; AAD06926.1; -. DR PIR; H64701; H64701. DR TIGR; HP1456; -. DR InterPro; IPR002217; Lipo_LPP20. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF02169; LPP20; 1. DR PRINTS; PR01019; LIPOLPP20. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 21 Probable. FT CHAIN 22 175 LPP20 lipoprotein. FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). FT VARIANT 16 16 A -> T (IN STRAIN NCTC 11638). FT VARIANT 152 152 V -> G (IN STRAIN NCTC 11638). SQ SEQUENCE 175 AA; 19108 MW; BBB8359E03C8458A CRC64; MKNQVKKILG MSVVAAMVIV GCSHAPKSGI SKSNKAYKEA TKGAPDWVVG DLEKVAKYEK YSGVFLGRAE DLITNNDVDY STNQATAKAR ANLAANLKST LQKDLENEKT RTVDASGKRS ISGTDTEKIS QLVDKELIAS KMLARYVGKD RVFVLVGLDK QIVDKVREEL GMVKK // ID LPPB_HAESO STANDARD; PRT; 337 AA. AC P36685; DT 01-JUN-1994 (Rel. 29, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Outer membrane antigenic lipoprotein B precursor (Fragment). GN LPPB. OS Haemophilus somnus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Histophilus. OX NCBI_TaxID=731; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HS25; RX MEDLINE=93239280; PubMed=8478068; RA Theisen M., Rioux C.R., Potter A.A.; RT "Molecular cloning, nucleotide sequence, and characterization of RT lppB, encoding an antigenic 40-kilodalton lipoprotein of Haemophilus RT somnus."; RL Infect. Immun. 61:1793-1798(1993). RN [2] RP CONCEPTUAL TRANSLATION. RA Bairoch A.; RL Unpublished observations (AUG-1995). CC -!- FUNCTION: MAY BE A VIRULENCE DETERMINANT. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- SIMILARITY: BELONGS TO THE E.COLI NLPD / HAEMOPHILUS LPPB FAMILY. CC -!- CAUTION: THIS IS A CONCEPTUAL TRANSLATION; THREE FRAMESHIFTS HAD CC TO BE INTRODUCED IN POSITIONS 264, 266 AND 328. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L10653; AAA72348.1; ALT_FRAME. DR MEROPS; M37.UPW; -. DR InterPro; IPR002482; LysM. DR InterPro; IPR002886; Peptidase_M37. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF01476; LysM; 1. DR Pfam; PF01551; Peptidase_M37; 1. DR SMART; SM00257; LysM; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Antigen; Virulence; Palmitate. FT SIGNAL 1 16 Probable. FT CHAIN 17 >337 Outer membrane antigenic lipoprotein B. FT LIPID 17 17 N-palmitoyl cysteine (Probable). FT LIPID 17 17 S-diacylglycerol cysteine (Probable). FT NON_TER 337 337 SQ SEQUENCE 337 AA; 36886 MW; B314FF9009AA3AD7 CRC64; MKKFLPLSIS ITVLAACSSH TPAPVENAKD LAPSIIKPIN GTNSTAWEPQ VIQQKMPESM RVPKATNSTY QPEIIQQNQQ KTESIAKKQA LQNFEIPRDP KTNVPVYSKI DKGFYKGDTY KVRKGDTMFL IAYISGMDIK ELATLNNMSE PYHLSIGQVL KIANNIPDSN MIPTQTINES EVTQNTVNET WNANKPTNEQ MKPVATPTHS TMPINKTPPA TSNIAWIWPT NGKIIQGFSS ADGGNKGIDI SGSRGQAVNA AAAGRVVYAG DALRGYGNLI IIKHNDSYLS AYAHNESILV KDQQEVKAGQ QIAKMGSSGT NTIKLHFXIR YFGQSVD // ID LPPL_PSEAE STANDARD; PRT; 46 AA. AC P17323; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lipopeptide precursor. GN LPPL OR PA5276. OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 15692 / PAO1; RX MEDLINE=90279511; PubMed=2112674; RA Jann A., Cavard D., Martin C., Cami B., Patte J.-C.; RT "A lipopeptide-encoding sequence upstream from the lysA gene of RT Pseudomonas aeruginosa."; RL Mol. Microbiol. 4:677-682(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 15692 / PAO1; RX MEDLINE=20437337; PubMed=10984043; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor (Probable). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51393; CAA35757.1; -. DR EMBL; AE004940; AAG08661.1; -. DR PIR; S10024; S10024. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Signal; Lipoprotein; Complete proteome; Palmitate. FT SIGNAL 1 20 FT CHAIN 21 46 Lipopeptide. FT LIPID 21 21 N-palmitoyl cysteine. FT LIPID 21 21 S-diacylglycerol cysteine. SQ SEQUENCE 46 AA; 5085 MW; 1CCA9D20FC712AFE CRC64; MKRLFLSFVA LALLAGSIAA CGQKGPLYLP DDEKAKKEHS KDRYGF // ID LYS4_ECOLI STANDARD; PRT; 52 AA. AC P09181; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lysis protein for colicin N precursor. GN CNL. OS Escherichia coli. OG Plasmid ColN pCHAP4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE=88174431; PubMed=3280946; RA Pugsley A.P.; RT "The immunity and lysis genes of ColN plasmid pCHAP4."; RL Mol. Gen. Genet. 211:335-341(1988). CC -!- FUNCTION: Lysis proteins are required for both colicin release and CC partial cell lysis. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06933; CAA30019.1; -. DR PIR; S01760; ZHECN4. DR InterPro; IPR003059; Lysis_col. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF02402; Lysis_col; 1. DR PRINTS; PR01297; LYSISCOLICIN. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Plasmid; Outer membrane; Lipoprotein; Signal; Palmitate. FT SIGNAL 1 17 Potential. FT CHAIN 18 52 Lysis protein for colicin N. FT LIPID 18 18 N-palmitoyl cysteine. FT LIPID 18 18 S-diacylglycerol cysteine. SQ SEQUENCE 52 AA; 5633 MW; F6F1BFE9BDAF81B6 CRC64; MCGKILLILF FIMTLSACQV NHIRDVKGGT VAPSSSSRLT GLKLSKRSKD PL // ID MLTA_VIBCH STANDARD; PRT; 368 AA. AC Q9KPQ4; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Membrane-bound lytic murein transglycosylase A precursor (EC 3.2.1.-) DE (Murein hydrolase A). GN MLTA OR VC2312. OS Vibrio cholerae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=666; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=El Tor N16961 / Serotype O1; RX MEDLINE=20406833; PubMed=10952301; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., RA Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D., RA Ermolaeva M.D., Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., RA McDonald L., Utterback T., Fleischmann R.D., Nierman W.C., White O., RA Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., RA Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). CC -!- FUNCTION: MUREIN-DEGRADING ENZYME. MAY PLAY A ROLE IN RECYCLING OF CC MUROPEPTIDES DURING CELL ELONGATION AND/OR CELL DIVISION. DEGRADES CC MUREIN GLYCAN STRANDS AND INSOLUBLE, HIGH-MOLECULAR WEIGHT MUREIN CC SACCULI (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: Cleavage of the beta-1,4-glycosidic bond CC between N-acetylmuramic acid and N-acetylglucosamine residues, CC thereby conserving the energy in a newly synthesized CC 1,6-anhydrobond in the muramic acid residue. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor (By similarity). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE004301; AAF95456.1; -. DR PIR; A82093; A82093. DR TIGR; VC2312; -. DR InterPro; IPR005300; MltA. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF03562; MltA; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Cell wall; Hydrolase; Glycosidase; Signal; Lipoprotein; KW Outer membrane; Complete proteome; Palmitate. FT SIGNAL 1 16 Probable. FT CHAIN 17 368 Membrane-bound lytic murein FT transglycosylase A. FT LIPID 17 17 N-palmitoyl cysteine (Probable). FT LIPID 17 17 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 368 AA; 40458 MW; C1341A9D21A41DBB CRC64; MSKRLLSLAS LALLFGCAQQ PNDRAQQYQQ QTFPHILNRA DVVESNKPRD YTEFSKQSEL VVQGSASMAK IYRPLYEQLN EWVLQSGDPA TLAQFGIQAA QLGGGDKQGN VLFTGYFSPV IELRHQPDSV FKYPVYGLPK CNKNCPTRAE IYQGALDGQG LELGYAENLI DPFIMEVQGS GFVHFGDDDT LEYFAYAGKN NKAYVSIGKV LIERGLVERE KMSLKAIKDW VLANDEATVR ELLEENPSFV FFKPSAAAPV KGSAGIPLLP MASVAGDRSI LPMGTPILAE VPLLNADGTW SGAHQLRLLI VLDTGGAVKQ NHLDLYHGMG PRAGLEAGHY KHFGRVWKLG LENSPTQAPW ALPPEKQQ // ID MLTB_ECOLI STANDARD; PRT; 361 AA. AC P41052; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Membrane-bound lytic murein transglycosylase B precursor (EC 3.2.1.-) DE (Murein hydrolase B) (35 kDa soluble lytic transglycosylase) (Slt35). GN MLTB OR B2701. OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE=96065704; PubMed=7476170; RA Ehlert K., Hoeltje J.-V., Templin M.F.; RT "Cloning and expression of a murein hydrolase lipoprotein from RT Escherichia coli."; RL Mol. Microbiol. 16:761-768(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95309413; PubMed=7789526; RA Dijkstra A.J., Hermann F., Keck W.; RT "Cloning and controlled overexpression of the gene encoding the 35 RT kDa soluble lytic transglycosylase from Escherichia coli."; RL FEBS Lett. 366:115-118(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE=97349980; PubMed=9205837; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., RA Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli RT - K12 genome corresponding to 50.0-68.8 min on the linkage map and RT analysis of its sequence features."; RL DNA Res. 4:91-113(1997). RN [5] RP PRELIMINARY SEQUENCE OF 1-91 FROM N.A. RX MEDLINE=87194727; PubMed=3553176; RA Yamada M., Saier M.H. Jr.; RT "Glucitol-specific enzymes of the phosphotransferase system in RT Escherichia coli. Nucleotide sequence of the gut operon."; RL J. Biol. Chem. 262:5455-5463(1987). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 42-361. RX MEDLINE=98437484; PubMed=9761817; RA van Asselt E.J., Perrakis A., Kalk K.H., Lamzin V.S., Dijkstra B.W.; RT "Accelerated X-ray structure elucidation of a 36 kDa RT muramidase/transglycosylase using wARP."; RL Acta Crystallogr. D 54:58-73(1998). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 40-361. RX MEDLINE=20035731; PubMed=10570954; RA van Asselt E.J., Dijkstra B.W.; RT "Binding of calcium in the EF-hand of Escherichia coli lytic RT transglycosylase Slt35 is important for stability."; RL FEBS Lett. 458:429-435(1999). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 40-361. RX MEDLINE=20015368; PubMed=10545329; RA van Asselt E.J., Dijkstra A.J., Kalk K.H., Takacs B., Keck W., RA Dijkstra B.W.; RT "Crystal structure of Escherichia coli lytic transglycosylase Slt35 RT reveals a lysozyme-like catalytic domain with an EF-hand."; RL Structure 7:1167-1180(1999). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 40-361. RX MEDLINE=20149813; PubMed=10684641; RA van Asselt E.J., Kalk K.H., Dijkstra B.W.; RT "Crystallographic studies of the interactions of Escherichia coli RT lytic transglycosylase Slt35 with peptidoglycan."; RL Biochemistry 39:1924-1934(2000). CC -!- FUNCTION: Murein-degrading enzyme. Catalyzes the cleavage of the CC glycosidic bonds between N-acetylmuramic acid and N- CC acetylglucosamine residues in peptidoglycan. May play a role in CC recycling of muropeptides during cell elongation and/or cell CC division. CC -!- CATALYTIC ACTIVITY: Cleavage of the beta-1,4-glycosidic bond CC between N-acetylmuramic acid and N-acetylglucosamine residues, CC thereby conserving the energy in a newly synthesized CC 1,6-anhydrobond in the muramic acid residue. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR AND EXPOSED TO THE PERIPLASMIC SIDE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18785; AAB60060.1; -. DR EMBL; AE000354; AAC75743.1; -. DR EMBL; D90892; BAA16563.1; -. DR EMBL; J02708; -; NOT_ANNOTATED_CDS. DR PIR; A65050; A65050. DR PDB; 1LTM; 11-NOV-98. DR PDB; 1QDR; 24-JAN-00. DR PDB; 1QDT; 24-JAN-00. DR PDB; 1QUS; 15-SEP-99. DR PDB; 1QUT; 15-SEP-99. DR PDB; 1D0K; 06-MAR-00. DR PDB; 1D0L; 06-MAR-00. DR PDB; 1D0M; 06-MAR-00. DR EcoGene; EG12699; mltB. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Cell wall; Hydrolase; Glycosidase; Signal; Lipoprotein; KW Outer membrane; Multigene family; 3D-structure; Complete proteome; KW Palmitate. FT SIGNAL 1 18 Probable. FT CHAIN 19 361 Membrane-bound lytic murein FT transglycosylase B. FT LIPID 19 19 N-palmitoyl cysteine (Probable). FT LIPID 19 19 S-diacylglycerol cysteine (Probable). FT ACT_SITE 162 162 FT TURN 45 46 FT TURN 53 56 FT HELIX 58 71 FT HELIX 75 82 FT TURN 83 84 FT HELIX 89 95 FT TURN 96 96 FT HELIX 113 118 FT TURN 119 121 FT HELIX 124 136 FT TURN 137 137 FT HELIX 138 148 FT HELIX 152 163 FT TURN 164 167 FT STRAND 172 173 FT HELIX 174 183 FT HELIX 186 188 FT HELIX 189 205 FT TURN 206 207 FT TURN 210 212 FT STRAND 214 215 FT TURN 217 218 FT STRAND 221 221 FT TURN 222 225 FT STRAND 226 226 FT HELIX 228 234 FT TURN 246 247 FT HELIX 249 262 FT TURN 263 264 FT TURN 267 268 FT STRAND 272 276 FT TURN 280 281 FT STRAND 285 291 FT HELIX 292 297 FT TURN 298 299 FT STRAND 301 302 FT TURN 307 308 FT STRAND 311 318 FT STRAND 323 328 FT HELIX 330 336 FT TURN 337 338 FT HELIX 342 361 SQ SEQUENCE 361 AA; 40256 MW; 7E98F040504F75F9 CRC64; MFKRRYVTLL PLFVLLAACS SKPKPTETDT TTGTPSGGFL LEPQHNVMQM GGDFANNPNA QQFIDKMVNK HGFDRQQLQE ILSQAKRLDS VLRLMDNQAP TTSVKPPSGP NGAWLRYRKK FITPDNVQNG VVFWNQYEDA LNRAWQVYGV PPEIIVGIIG VETRWGRVMG KTRILDALAT LSFNYPRRAE YFSGELETFL LMARDEQDDP LNLKGSFAGA MGYGQFMPSS YKQYAVDFSG DGHINLWDPV DAIGSVANYF KAHGWVKGDQ VAVMANGQAP GLPNGFKTKY SISQLAAAGL TPQQPLGNHQ QASLLRLDVG TGYQYWYGLP NFYTITRYNH STHYAMAVWQ LGQAVALARV Q // ID MP17_FRATU STANDARD; PRT; 149 AA. AC P18149; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 17 kDa major membrane protein precursor (TUL4). OS Francisella tularensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=263; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=LVS; RX MEDLINE=90293477; PubMed=1694206; RA Sjoestedt A., Sandstroem G., Taernvik A., Jaurin B.; RT "Nucleotide sequence and T cell epitopes of a membrane protein of RT Francisella tularensis."; RL J. Immunol. 145:311-317(1990). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32059; AAA24919.1; -. DR PIR; B37169; B37169. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Palmitate. FT SIGNAL 1 19 Probable. FT CHAIN 20 149 17 kDa major membrane protein. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 149 AA; 15772 MW; B0689B3FBCB9FF29 CRC64; MKKIIKLSLL SLSIAGLASC STLGLGGSDD AKASAKDTAA AQTATTEQAA AVSKPTAKVS LNKLGQDKIK ATVYTAYNNN PQGSVRLQWQ APEGSKCHDT SFPITKYAEK NDKTWATVTV KQGNNFCSGK WTANVVYDKE VIASDSINI // ID MULI_MORMO STANDARD; PRT; 78 AA. AC P02940; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Major outer membrane lipoprotein precursor (Murein-lipoprotein). GN LPP. OS Morganella morganii (Proteus morganii). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Morganella. OX NCBI_TaxID=582; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83238418; PubMed=6305973; RA Huang Y.-X., Ching G., Inouye M.; RT "Comparison of the lipoprotein gene among the enterobacteriaceae. DNA RT sequence of Morganella morganii lipoprotein gene and its expression RT in Escherichia coli."; RL J. Biol. Chem. 258:8139-8145(1983). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K00084; AAA25322.1; -. DR PIR; A03440; LPEBWM. DR HSSP; P02937; 1MLP. DR InterPro; IPR006817; LPP. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF04728; LPP; 2. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Signal; Lipoprotein; Repeat; Palmitate. FT SIGNAL 1 20 FT CHAIN 21 78 Major outer membrane lipoprotein. FT LIPID 21 21 N-palmitoyl cysteine. FT LIPID 21 21 S-diacylglycerol cysteine. FT REPEAT 24 34 FT REPEAT 38 48 SQ SEQUENCE 78 AA; 8430 MW; 2BB4EC7DF2164543 CRC64; MGRSKIVLGA VVLASALLAG CSSNAKFDQL DNDVKTLNAK VDQLSNDVNA IRADVQQAKD EAARANQRLD NQVRSYKK // ID MULI_PROMI STANDARD; PRT; 78 AA. AC P09461; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Major outer membrane lipoprotein precursor (Murein-lipoprotein). GN LPP. OS Proteus mirabilis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Proteus. OX NCBI_TaxID=584; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86168162; PubMed=3007466; RA Ching G., Inouye M.; RT "Expression of the Proteus mirabilis lipoprotein gene in Escherichia RT coli. Existence of tandem promoters."; RL J. Biol. Chem. 261:4600-4606(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=86037225; PubMed=3903165; RA Ching G., Inouye M.; RT "Evolution of the lipoprotein gene in the enterobacteriaceae. Cloning RT and DNA sequence of the lpp gene from Proteus mirabilis."; RL J. Mol. Biol. 185:501-507(1985). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M13176; AAA25658.1; -. DR EMBL; M28554; AAA25659.1; -. DR PIR; A24352; A24352. DR HSSP; P02937; 1MLP. DR InterPro; IPR006817; LPP. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF04728; LPP; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Signal; Lipoprotein; Repeat; Palmitate. FT SIGNAL 1 19 FT CHAIN 20 78 Major outer membrane lipoprotein. FT LIPID 20 20 N-palmitoyl cysteine. FT LIPID 20 20 S-diacylglycerol cysteine. FT REPEAT 24 34 FT REPEAT 38 48 SQ SEQUENCE 78 AA; 8251 MW; 728C5B18E7682B94 CRC64; MKAKIVLGAV ILASGLLAGC SSSNNAQLDQ ISSDVNRLNT QVQQLSSDVQ SANAQAKAAY EAARANQRLD NQVTTYKK // ID MULI_PSEAE STANDARD; PRT; 83 AA. AC P11221; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Major outer membrane lipoprotein precursor (Murein-lipoprotein) DE (Lipoprotein I). GN OPRI OR PA2853. OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Isolate PA2; RX MEDLINE=89313294; PubMed=2473376; RA Cornelis P., Bouia A., Belarbi A., Guyonvarch A., Kammerer B., RA Hannaert V., Hubert J.-C.; RT "Cloning and analysis of the gene for the major outer membrane RT lipoprotein from Pseudomonas aeruginosa."; RL Mol. Microbiol. 3:421-428(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=89327122; PubMed=2502533; RA Duchene M., Barron C., Schweizer A., von Sprecht B.-U., Domdey H.; RT "Pseudomonas aeruginosa outer membrane lipoprotein I gene: molecular RT cloning, sequence, and expression in Escherichia coli."; RL J. Bacteriol. 171:4130-4137(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 15692 / PAO1; RX MEDLINE=92268853; PubMed=1588307; RA Saint-Onge A., Romeyer F., Lebel P., Masson L., Brousseau R.; RT "Specificity of the Pseudomonas aeruginosa PAO1 lipoprotein I gene as RT a DNA probe and PCR target region within the Pseudomonadaceae."; RL J. Gen. Microbiol. 138:733-741(1992). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 15692 / PAO1; RX MEDLINE=20437337; PubMed=10984043; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13748; CAA32013.1; -. DR EMBL; M25761; AAA25880.1; -. DR EMBL; X58714; CAA41550.1; -. DR EMBL; A07695; CAA00707.1; -. DR EMBL; AE004712; AAG06241.1; -. DR PIR; A33854; A33854. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 19 FT CHAIN 20 83 Major outer membrane lipoprotein. FT LIPID 20 20 N-palmitoyl cysteine. FT LIPID 20 20 S-diacylglycerol cysteine. SQ SEQUENCE 83 AA; 8835 MW; E87F52B86B04DBA4 CRC64; MNNVLKFSAL ALAAVLATGC SSHSKETEAR LTATEDAAAR AQARADEAYR KADEALGAAQ KAQQTADEAN ERALRMLEKA SRK // ID NLPA_ECOLI STANDARD; PRT; 272 AA. AC P04846; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lipoprotein-28 precursor. GN NLPA OR B3661. OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86111928; PubMed=3003106; RA Yu F., Inouye S., Inouye M.; RT "Lipoprotein-28, a cytoplasmic membrane lipoprotein from Escherichia RT coli. Cloning, DNA sequence, and expression of its gene."; RL J. Biol. Chem. 261:2284-2288(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=93315143; PubMed=7686882; RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.; RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli RT genome: organizational symmetry around the origin of replication."; RL Genomics 16:551-561(1993). CC -!- SUBCELLULAR LOCATION: Attached to the inner membrane by a lipid CC anchor. CC -!- SIMILARITY: Belongs to the nlpA lipoprotein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12163; AAA24080.1; -. DR EMBL; L10328; AAA62013.1; -. DR EMBL; AE000443; AAC76684.1; -. DR PIR; A26286; LPEC28. DR SWISS-2DPAGE; P04846; COLI. DR EcoGene; EG10657; nlpA. DR InterPro; IPR004872; Lipoprotein_9. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR004478; YaeC. DR Pfam; PF03180; Lipoprotein_9; 1. DR TIGRFAMs; TIGR00363; TIGR00363; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Inner membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 23 FT CHAIN 24 272 Lipoprotein-28. FT LIPID 24 24 N-palmitoyl cysteine. FT LIPID 24 24 S-diacylglycerol cysteine. SQ SEQUENCE 272 AA; 29423 MW; E3C249E753AB1B33 CRC64; MKLTTHHLRT GAALLLAGIL LAGCDQSSSD AKHIKVGVIN GAEQDVAEVA KKVAKEKYGL DVELVGFSGS LLPNDATNHG ELDANVFQHR PFLEQDNQAH GYKLVAVGNT FVFPMAGYSK KIKTVAQIKE GATVAIPNDP TNLGRALLLL QKEKLITLKE GKGLLPTALD ITDNPRHLQI MELEGAQLPR VLDDPKVDVA IISTTYIQQT GLSPVHDSVF IEDKNSPYVN ILVAREDNKN AENVKEFLQS YQSPEVAKAA ETIFNGGAVP GW // ID NLPB_ECOLI STANDARD; PRT; 344 AA. AC P21167; P76564; DT 01-MAY-1991 (Rel. 18, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lipoprotein-34 precursor. GN NLPB OR DAPX OR B2477 OR SF2520 OR S2670. OS Escherichia coli, and OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562, 623; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12; RX MEDLINE=91358331; PubMed=1885529; RA Bouvier J., Pugsley A.P., Stragier P.; RT "A gene for a new lipoprotein in the dapA-purC interval of the RT Escherichia coli chromosome."; RL J. Bacteriol. 173:5523-5531(1991). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12; RX MEDLINE=91008982; PubMed=2120198; RA Tiedemann A.A., Demarini D.J., Parker J., Smith J.M.; RT "DNA sequence of the purC gene encoding 5'-phosphoribosyl-5- RT aminoimidazole-4-N-succinocarboxamide synthetase and organization of RT the dapA-purC region of Escherichia coli K-12."; RL J. Bacteriol. 172:6035-6041(1990). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12; RX MEDLINE=97349980; PubMed=9205837; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., RA Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli RT - K12 genome corresponding to 50.0-68.8 min on the linkage map and RT analysis of its sequence features."; RL DNA Res. 4:91-113(1997). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=2457T / ATCC 700930 / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- FUNCTION: Non-essential lipoprotein. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- CAUTION: Ref.2 sequence differs from that shown due to CC frameshifts. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57402; CAA40661.1; -. DR EMBL; M33928; -; NOT_ANNOTATED_CDS. DR EMBL; AE000335; AAC75530.1; ALT_INIT. DR EMBL; D90876; BAA16354.1; -. DR EMBL; D90877; BAA16364.1; -. DR EMBL; AE015267; AAN44023.1; ALT_INIT. DR EMBL; AE016986; AAP17837.1; -. DR PIR; D65023; D65023. DR SWISS-2DPAGE; P21167; COLI. DR EcoGene; EG10658; nlpB. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 24 FT CHAIN 25 344 Lipoprotein-34. FT LIPID 25 25 N-palmitoyl cysteine. FT LIPID 25 25 S-diacylglycerol cysteine. SQ SEQUENCE 344 AA; 36842 MW; 49991F277D9D923C CRC64; MAYSVQKSRL AKVAGVSLVL LLAACSSDSR YKRQVSGDEA YLEAAPLAEL HAPAGMILPV TSGDYAIPVT NGSGAVGKAL DIRPPAQPLA LVSGARTQFT GDTASLLVEN GRGNTLWPQV VSVLQAKNYT ITQRDDAGQT LTTDWVQWNR LDEDEQYRGR YQISVKPQGY QQAVTVKLLN LEQAGKPVAD AASMQRYSTE MMNVISAGLD KSATDAANAA QNRASTTMDV QSAADDTGLP MLVVRGPFNV VWQRLPAALE KVGMKVTDST RSQGNMAVTY KPLSDSDWQE LGASDPGLAS GDYKLQVGDL DNRSSLQFID PKGHTLTQSQ NDALVAVFQA AFSK // ID NLPD_ECOLI STANDARD; PRT; 379 AA. AC P33648; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lipoprotein nlpD precursor. GN NLPD OR B2742 OR SF2765 OR S2958. OS Escherichia coli, and OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562, 623; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=MP180; RX MEDLINE=94179096; PubMed=8132457; RA Ichikawa J.K., Li C., Fu J.C., Clarke S.; RT "A gene at 59 minutes on the Escherichia coli chromosome encodes a RT lipoprotein with unusual amino acid repeat sequences."; RL J. Bacteriol. 176:1630-1638(1994). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [3] RP SEQUENCE OF 99-379 FROM N.A. RC SPECIES=E.coli; STRAIN=K12 / DH1; RX MEDLINE=94268497; PubMed=8208244; RA Takayanagi Y., Tanaka K., Takahashi H.; RT "Structure of the 5' upstream region and the regulation of the rpoS RT gene of Escherichia coli."; RL Mol. Gen. Genet. 243:525-531(1994). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=2457T / ATCC 700930 / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- FUNCTION: May be involved in stationary-phase survival. CC -!- SUBCELLULAR LOCATION: Attached to the inner membrane by a lipid CC anchor (Potential). CC -!- SIMILARITY: BELONGS TO THE E.COLI NLPD / HAEMOPHILUS LPPB FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L07869; AAA17875.1; -. DR EMBL; U29579; AAA69252.1; -. DR EMBL; AE000358; AAC75784.1; -. DR EMBL; D17549; BAA04487.1; -. DR EMBL; AE015290; AAN44254.1; ALT_INIT. DR EMBL; AE016987; AAP18080.1; -. DR PIR; B55522; B55522. DR MEROPS; M37.UPW; -. DR SWISS-2DPAGE; P33648; COLI. DR EcoGene; EG12111; nlpD. DR InterPro; IPR002482; LysM. DR InterPro; IPR002886; Peptidase_M37. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF01476; LysM; 1. DR Pfam; PF01551; Peptidase_M37; 1. DR SMART; SM00257; LysM; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Inner membrane; Lipoprotein; Repeat; Signal; Complete proteome; KW Palmitate. FT SIGNAL 1 25 FT CHAIN 26 379 Lipoprotein nlpD. FT LIPID 26 26 N-palmitoyl cysteine. FT LIPID 26 26 S-diacylglycerol cysteine. FT DOMAIN 66 97 4 X 8 AA TANDEM REPEATS OF Q-Q-P-Q-I-Q- FT P-V. FT REPEAT 66 73 1-1. FT REPEAT 74 81 1-2 (approximate). FT REPEAT 82 89 1-3. FT REPEAT 90 97 1-4 (APPROXIMATE). FT DOMAIN 205 252 4 X 7 AA APPROXIMATE REPEATS. FT REPEAT 205 211 2-1. FT REPEAT 227 233 2-2. FT REPEAT 239 245 2-3. FT REPEAT 246 252 2-4. FT CONFLICT 139 139 G -> A (in Ref. 3). SQ SEQUENCE 379 AA; 40149 MW; A8E6A2B8456105FE CRC64; MSAGSPKFTV RRIAALSLVS LWLAGCSDTS NPPAPVSSVN GNAPANTNSG MLITPPPKMG TTSTAQQPQI QPVQQPQIQA TQQPQIQPVQ PVAQQPVQME NGRIVYNRQY GNIPKGSYSG STYTVKKGDT LFYIAWITGN DFRDLAQRNN IQAPYALNVG QTLQVGNASG TPITGGNAIT QADAAEQGVV IKPAQNSTVA VASQPTITYS ESSGEQSANK MLPNNKPTAT TVTAPVTVPT ASTTEPTVSS TSTSTPISTW RWPTEGKVIE TFGASEGGNK GIDIAGSKGQ AIIATADGRV VYAGNALRGY GNLIIIKHND DYLSAYAHND TMLVREQQEV KAGQKIATMG STGTSSTRLH FEIRYKGKSV NPLRYLPQR // ID NLPD_PSEAE STANDARD; PRT; 297 AA. AC P45682; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lipoprotein nlpD/lppB homolog precursor. GN PA3623. OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 15692 / PAO1; RX MEDLINE=95047554; PubMed=7959068; RA Tanaka K., Takahashi H.; RT "Cloning, analysis and expression of an rpoS homologue gene from RT Pseudomonas aeruginosa PAO1."; RL Gene 150:81-85(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 15692 / PAO1; RX MEDLINE=20437337; PubMed=10984043; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- SUBCELLULAR LOCATION: Attached to the inner membrane by a lipid CC anchor (Potential). CC -!- SIMILARITY: BELONGS TO THE E.COLI NLPD / HAEMOPHILUS LPPB FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D26134; BAA05130.1; -. DR EMBL; AE004782; AAG07011.1; -. DR PIR; S55063; S55063. DR MEROPS; M37.UPW; -. DR InterPro; IPR002482; LysM. DR InterPro; IPR002886; Peptidase_M37. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF01476; LysM; 1. DR Pfam; PF01551; Peptidase_M37; 1. DR SMART; SM00257; LysM; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; FALSE_NEG. KW Inner membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 22 Probable. FT CHAIN 23 297 Lipoprotein nlpD/lppB homolog. FT LIPID 23 23 N-palmitoyl cysteine (Probable). FT LIPID 23 23 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 297 AA; 30835 MW; 2CDFD26FF4CBC704 CRC64; MDKGEGLRLA ATLRQWTRLY GGCHLLLGAV VCSLLAACSS SPPGGVKVVD RNGSAPAAAR RTPVTSGQYI VRRGDTLYSI AFRFGWDWKA LAARNGIAPP YTIQVGQAIQ FGGRASTQPS VAKNTPVVAA PVATKPTPVP PAVSTSVPAK PAPAPASTTT PPSSGATPVV AGPAVGGWAW PASGTLIGRF ASNGSLNKGI DIAGQLGQPV LAASGGTVVY AGSGLRGYGE LVIIKHNETY VSAYGHNRRL LVREGQQVKV GQSIAEMGST GTDRVKLHFE IRRQGKPVDP LQYLPRR // ID NLPI_ECOLI STANDARD; PRT; 294 AA. AC P39833; DT 01-FEB-1995 (Rel. 31, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Lipoprotein nlpI precursor. GN NLPI OR B3163 OR C3918 OR Z4524 OR ECS4044 OR SF3204 OR S3421. OS Escherichia coli, OS Escherichia coli O6, OS Escherichia coli O157:H7, and OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562, 217992, 83334, 623; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [2] RP PRELIMINARY SEQUENCE FROM N.A. RC SPECIES=E.coli; RX MEDLINE=91258309; PubMed=2045359; RA Toone M.W., Rudd K.E., Friesen J.D.; RT "deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RT RNA helicase, can suppress a mutation in rpsB, the gene encoding RT ribosomal protein S2."; RL J. Bacteriol. 173:3291-3302(1991). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O6:H1 / CFT073 / ATCC 700928; RX MEDLINE=22388234; PubMed=12471157; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O157:H7 / EDL933 / ATCC 700927; RX MEDLINE=21074935; PubMed=11206551; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O157:H7 / RIMD 0509952; RX MEDLINE=21156231; PubMed=11258796; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). RN [6] RP SEQUENCE OF 1-41 FROM N.A. RC SPECIES=E.coli; STRAIN=JCH5/JC553; RX MEDLINE=87083499; PubMed=2432069; RA Regnier P., Grunberg-Manago M., Portier C.; RT "Nucleotide sequence of the pnp gene of Escherichia coli encoding RT polynucleotide phosphorylase. Homology of the primary structure of RT the protein with the RNA-binding domain of ribosomal protein S1."; RL J. Biol. Chem. 262:63-68(1987). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=2457T / ATCC 700930 / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). RN [9] RP IDENTIFICATION. RC SPECIES=E.coli; RX MEDLINE=95075659; PubMed=7984428; RA Borodovsky M., Rudd K.E., Koonin E.V.; RT "Intrinsic and extrinsic approaches for detecting genes in a RT bacterial genome."; RL Nucleic Acids Res. 22:4756-4767(1994). RN [10] RP CHARACTERIZATION. RC SPECIES=E.coli; STRAIN=K12; RX MEDLINE=99328978; PubMed=10400590; RA Ohara M., Wu H.C., Sankaran K., Rick P.D.; RT "Identification and characterization of a new lipoprotein, NlpI, in RT Escherichia coli K-12."; RL J. Bacteriol. 181:4318-4325(1999). CC -!- FUNCTION: MAY BE INVOLVED IN CELL DIVISION. OVEREXPRESSION OF NLPI CC RESULTS IN THE LOSS OF THE ROD MORPHOLOGY AND THE FORMATION OF CC SINGLE PROLATE ELLIPSOIDS AND PAIRS OF PROLATE ELLIPSOIDS JOINED CC BY PARTIAL CONSTRICTIONS. CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor. CC -!- SIMILARITY: Contains 3 TPR repeats. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18997; AAA57966.1; -. DR EMBL; AE000397; AAC76197.1; -. DR EMBL; M63288; -; NOT_ANNOTATED_CDS. DR EMBL; AE016767; AAN82359.1; -. DR EMBL; AE005545; AAG58299.1; -. DR EMBL; AP002564; BAB37467.1; -. DR EMBL; J02638; AAA83906.1; -. DR EMBL; AE015332; AAN44671.1; ALT_INIT. DR EMBL; AE016989; AAP18485.1; -. DR PIR; D91134; D91134. DR PIR; G65106; G65106. DR PIR; G85979; G85979. DR EcoGene; EG12371; nlpI. DR InterPro; IPR008940; Prenyl_trans. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR001440; TPR. DR Pfam; PF00515; TPR; 3. DR SMART; SM00028; TPR; 3. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS50005; TPR; 3. DR PROSITE; PS50293; TPR_REGION; 2. KW Cell division; Membrane; Lipoprotein; Repeat; TPR repeat; Signal; KW Complete proteome; Palmitate. FT SIGNAL 1 18 FT CHAIN 19 294 Lipoprotein nlpI. FT LIPID 19 19 N-palmitoyl cysteine. FT LIPID 19 19 S-diacylglycerol cysteine. FT REPEAT 62 95 TPR 1. FT REPEAT 96 129 TPR 2. FT REPEAT 130 163 TPR 3. FT CONFLICT 103 103 G -> A (in Ref. 2). SQ SEQUENCE 294 AA; 33620 MW; 4CA6724327A9CEE7 CRC64; MKPFLRWCFV ATALTLAGCS NTSWRKSEVL AVPLQPTLQQ EVILARMEQI LASRALTDDE RAQLLYERGV LYDSLGLRAL ARNDFSQALA IRPDMPEVFN YLGIYLTQAG NFDAAYEAFD SVLELDPTYN YAHLNRGIAL YYGGRDKLAQ DDLLAFYQDD PNDPFRSLWL YLAEQKLDEK QAKEVLKQHF EKSDKEQWGW NIVEFYLGNI SEQTLMERLK ADATDNTSLA EHLSETNFYL GKYYLSLGDL DSATALFKLA VANNVHNFVE HRYALLELSL LGQDQDDLAE SDQQ // ID OMLA_ACTPL STANDARD; PRT; 365 AA. AC Q02937; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Outer membrane lipoprotein A precursor. GN OMLA. OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=715; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Serotype 1 / Isolate AP37; RX MEDLINE=93138779; PubMed=8423086; RA Gerlach G.-F., Anderson C., Klashinsky S., Rossi-Campos A., RA Potter A.A., Willson P.J.; RT "Molecular characterization of a protective outer membrane RT lipoprotein (OmlA) from Actinobacillus pleuropneumoniae serotype 1."; RL Infect. Immun. 61:565-572(1993). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L06318; AAC41456.1; -. DR PIR; A49235; A49235. DR InterPro; IPR005014; Lipoprotein_14. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF03346; Lipoprotein_14; 1. DR ProDom; PD023715; Lipoprotein_14; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Signal; Lipoprotein; Palmitate. FT SIGNAL 1 19 FT CHAIN 20 365 Outer membrane lipoprotein A. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 365 AA; 39784 MW; 20D4B3FAEBE2842F CRC64; MNIATKLMAS LVASVVLTAC SGGGSSGSSS KPNSELTPKV DMSAPKAEQP KKEEVPQADN SKAEEPKEMA PQVDSPKAEE PKNMAPQMGN PKLNDPQVMA PKMDNPQKDA PKGEELSKDK SNAEILKELG VKDINSGIIN NADVVLNLKI DEKDHITVVL DKGKINRNHL KVTNTISAQD IKTLKDSSGK LLGYYGYMQL NQVRQDENYS DEKVSLNEYY LLSMNDADKI RPTKSISYKG DMFYSYKDVG NQKLKASVEA SYDDVTKKVS MKVFGENNDY WKLGEFGRTN LLENQVTGAK VGEDGTIING TLYSKIDNFP LKLTPDANFS GGIFGKNGEV LAGSAISEKW QGVIGATATT KEDKK // ID OMLA_PSEAE STANDARD; PRT; 176 AA. AC O68562; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Outer membrane lipoprotein omlA precursor. GN OMLA OR OPRX OR PA4765. OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 15692 / PAO1; RX MEDLINE=99138728; PubMed=9973334; RA Ochsner U.A., Vasil A.I., Johnson Z., Vasil M.L.; RT "Pseudomonas aeruginosa fur overlaps with a gene encoding a novel RT outer membrane lipoprotein, OmlA."; RL J. Bacteriol. 181:1099-1109(1999). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 15692 / PAO1; RX MEDLINE=20437337; PubMed=10984043; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: MAY HAVE A STRUCTURAL ROLE IN MAINTAINING THE CELL CC ENVELOPE INTEGRITY. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- SIMILARITY: Belongs to the smpA/omlA family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF050676; AAC05678.1; -. DR EMBL; AE004890; AAG08151.1; -. DR PIR; A83050; A83050. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR007450; SmpA_OmlA. DR Pfam; PF04355; SmpA_OmlA; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 21 FT CHAIN 22 176 Outer membrane lipoprotein omlA. FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). FT DOMAIN 162 176 Pro-rich. SQ SEQUENCE 176 AA; 19395 MW; 254A64F50735B1EB CRC64; MQNAKLMLTC LAFAGLAALA GCSFPGVYKI DIQQGNVVTQ DMIDQLRPGM TRRQVRFIMG NPLIVDTFHA NRWDYLYSIQ PGGGRRQQER VSLFFNDSDQ LAGLNGDFMP GVSRDEAILG KEGSTTVTQP ADQQKPEAQK EEPPKPGSTL EQLQREVDEA QPVPVPTPEP LDPSPQ // ID OSA1_BORBU STANDARD; PRT; 273 AA. AC P14013; Q44882; Q57272; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Outer surface protein A precursor. GN OSPA OR BBA15. OS Borrelia burgdorferi (Lyme disease spirochete). OG Plasmid lp54. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=139; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ZS7; RX MEDLINE=90067859; PubMed=2587225; RA Wallich R., Schaible U.E., Simon M.M., Heiberger A., Kramer M.D.; RT "Cloning and sequencing of the gene encoding the outer surface RT protein A (OspA) of a European Borrelia burgdorferi isolate."; RL Nucleic Acids Res. 17:8864-8864(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 35210 / B31; RX MEDLINE=89343634; PubMed=2761388; RA Bergstroem S., Bundoc V., Barbour A.G.; RT "Molecular analysis of linear plasmid-encoded major surface proteins, RT OspA and OspB, of the Lyme disease spirochaete Borrelia RT burgdorferi."; RL Mol. Microbiol. 3:479-486(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=N40; RX MEDLINE=92185237; PubMed=1545130; RA Fikrig E., Barthold S.W., Persing D.H., Sun X., Kantor F.S., RA Flavell R.A.; RT "Borrelia burgdorferi strain 25015: characterization of outer surface RT protein A and vaccination against infection."; RL J. Immunol. 148:2256-2260(1992). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=PBRE, and KA; RX MEDLINE=96085967; PubMed=7500914; RA Will G., Jauris-Heipke S., Schwab E., Busch U., Roessler D., RA Soutschek E., Wilske B., Preac-Mursic V.; RT "Sequence analysis of ospA genes shows homogeneity within Borrelia RT burgdorferi sensu stricto and Borrelia afzelii strains but reveals RT major subgroups within the Borrelia garinii species."; RL Med. Microbiol. Immunol. 184:73-80(1995). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=KA; RX MEDLINE=94052124; PubMed=8234271; RA Dykhuizen D.E., Polin D.S., Dunn J.J., Wilske B., Preac-Mursic V., RA Dattwyler R.J., Luft B.J.; RT "Borrelia burgdorferi is clonal: implications for taxonomy and vaccine RT development."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10163-10167(1993). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 35210 / B31; RX MEDLINE=98065943; PubMed=9403685; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., RA Dougherty B., Tomb J.-F., Fleischmann R.D., Richardson D., RA Peterson J., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J., RA Utterback T., Watthey L., McDonald L., Artiach P., Bowman C., RA Garland S., Fujii C., Cotton M.D., Horst K., Roberts K., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS). RX MEDLINE=97268612; PubMed=9108020; RA Li H., Dunn J.J., Luft B.J., Lawson C.L.; RT "Crystal structure of Lyme disease antigen outer surface protein A RT complexed with an Fab."; RL Proc. Natl. Acad. Sci. U.S.A. 94:3584-3589(1997). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS). RC STRAIN=ATCC 35210 / B31; RX MEDLINE=20500110; PubMed=11183781; RA Ding W., Huang X., Yang X., Dunn J.J., Luft B.J., Koide S., RA Lawson C.L.; RT "Structural identification of a key protective B-cell epitope in Lyme RT disease antigen OspA."; RL J. Mol. Biol. 302:1153-1164(2000). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- MISCELLANEOUS: THE SEQUENCE SHOWN IS THAT OF STRAIN ZS7. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16467; CAA34487.1; -. DR EMBL; X14407; CAA32579.1; -. DR EMBL; M57248; -; NOT_ANNOTATED_CDS. DR EMBL; A22442; CAA01606.1; -. DR EMBL; X85739; CAA59742.1; -. DR EMBL; X80182; CAA56467.1; -. DR EMBL; X69606; CAA49314.1; -. DR EMBL; A04009; CAA00316.1; -. DR EMBL; AE000790; AAC66260.1; -. DR PIR; F49209; F49209. DR PIR; G70208; G70208. DR PIR; S14906; MMLYAZ. DR PIR; S71529; S71529. DR PDB; 1OSP; 21-APR-97. DR PDB; 1FJ1; 11-OCT-00. DR TIGR; BBA15; -. DR InterPro; IPR001809; Outrsurface. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00820; Lipoprotein_1; 1. DR PRINTS; PR00968; OUTRSURFACE. DR ProDom; PD001127; Outrsurface; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Plasmid; 3D-structure; KW Complete proteome; Palmitate. FT SIGNAL 1 16 FT CHAIN 17 273 Outer surface protein A. FT LIPID 17 17 N-palmitoyl cysteine (Probable). FT LIPID 17 17 S-diacylglycerol cysteine (Probable). FT VARIANT 39 39 N -> K (IN STRAINS B31 AND KA). FT VARIANT 114 114 V -> A (IN STRAIN PBRE). FT VARIANT 149 149 E -> G (IN STRAINS B31 AND KA). FT VARIANT 164 164 S -> G (IN STRAINS B31, N40 AND KA). FT HELIX 26 28 FT STRAND 29 33 FT HELIX 35 37 FT STRAND 39 43 FT TURN 48 49 FT STRAND 52 58 FT TURN 59 60 FT STRAND 61 67 FT STRAND 74 79 FT TURN 81 82 FT STRAND 85 90 FT TURN 92 93 FT STRAND 96 102 FT TURN 104 105 FT STRAND 109 116 FT TURN 117 118 FT STRAND 121 126 FT TURN 128 129 FT STRAND 132 138 FT TURN 140 141 FT STRAND 144 148 FT TURN 152 153 FT STRAND 156 161 FT STRAND 166 171 FT STRAND 175 182 FT TURN 183 184 FT STRAND 185 192 FT TURN 193 194 FT STRAND 197 203 FT TURN 208 210 FT STRAND 212 217 FT HELIX 218 220 FT TURN 221 221 FT STRAND 222 227 FT TURN 228 229 FT STRAND 230 237 FT TURN 239 240 FT STRAND 243 248 FT TURN 250 251 FT STRAND 255 255 FT STRAND 260 261 FT HELIX 265 273 SQ SEQUENCE 273 AA; 29455 MW; 0889191B09F45EC2 CRC64; MKKYLLGIGL ILALIACKQN VSSLDEKNSV SVDLPGEMNV LVSKEKNKDG KYDLIATVDK LELKGTSDKN NGSGVLEGVK ADKSKVKLTI SDDLGQTTLE VFKEDGKTLV SKKVTSKDKS STEEKFNEKG EVSEKIITRA DGTRLEYTEI KSDGSGKAKE VLKSYVLEGT LTAEKTTLVV KEGTVTLSKN ISKSGEVSVE LNDTDSSAAT KKTAAWNSGT STLTITVNSK KTKDLVFTKE NTITVQQYDS NGTKLEGSAV EITKLDEIKN ALK // ID OSB1_BORBU STANDARD; PRT; 296 AA. AC P17739; O50909; Q44963; Q44965; Q44966; Q44968; Q44970; Q44972; AC Q44975; Q57510; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Outer surface protein B precursor. GN OSPB OR BBA16. OS Borrelia burgdorferi (Lyme disease spirochete). OG Plasmid lp54. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=139; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 35210 / B31; RX MEDLINE=89343634; PubMed=2761388; RA Bergstroem S., Bundoc V., Barbour A.G.; RT "Molecular analysis of linear plasmid-encoded major surface proteins, RT OspA and OspB, of the Lyme disease spirochaete Borrelia RT burgdorferi."; RL Mol. Microbiol. 3:479-486(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Various strains; RX MEDLINE=94166630; PubMed=8121286; RA Caporale D.A., Kocher T.D.; RT "Sequence variation in the outer-surface-protein genes of Borrelia RT burgdorferi."; RL Mol. Biol. Evol. 11:51-64(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=HB19; RX MEDLINE=94222578; PubMed=7513309; RA Sadziene A., Jonsson M., Bergstroem S., Bright R.K., Kennedy R.C., RA Barbour A.G.; RT "A bactericidal antibody to Borrelia burgdorferi is directed against RT a variable region of the OspB protein."; RL Infect. Immun. 62:2037-2045(1994). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 35210 / B31; RX MEDLINE=98065943; PubMed=9403685; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., RA Dougherty B., Tomb J.-F., Fleischmann R.D., Richardson D., RA Peterson J., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J., RA Utterback T., Watthey L., McDonald L., Artiach P., Bowman C., RA Garland S., Fujii C., Cotton M.D., Horst K., Roberts K., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14407; CAA32580.1; -. DR EMBL; L23136; AAA22952.1; -. DR EMBL; L23137; AAA22954.1; -. DR EMBL; L23138; AAA20948.1; -. DR EMBL; L23139; AAA20950.1; -. DR EMBL; L23140; AAA20952.1; -. DR EMBL; L23141; AAA20954.1; -. DR EMBL; L23142; AAA20956.1; -. DR EMBL; L23143; AAA20958.1; -. DR EMBL; L23144; AAA20960.1; -. DR EMBL; L31399; AAA63758.1; -. DR EMBL; AE000790; AAC66243.1; -. DR PIR; I40250; I40250. DR PIR; I40252; I40252. DR PIR; I40256; I40256. DR PIR; I40260; I40260. DR PIR; I40264; I40264. DR TIGR; BBA16; -. DR InterPro; IPR001809; Outrsurface. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00820; Lipoprotein_1; 1. DR PRINTS; PR00968; OUTRSURFACE. DR ProDom; PD001127; Outrsurface; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Plasmid; Complete proteome; KW Palmitate. FT SIGNAL 1 15 FT CHAIN 16 296 Outer surface protein B. FT LIPID 16 16 N-palmitoyl cysteine (Probable). FT LIPID 16 16 S-diacylglycerol cysteine (Probable). FT VARIANT 42 42 H -> Y (IN STRAIN CA7). FT VARIANT 89 89 K -> R (IN STRAIN 41552MA). FT VARIANT 123 123 T -> S (IN STRAIN CA8). FT VARIANT 126 126 A -> T (IN STRAINS 21343WI, 41552MA, FT 42373NY3, HB19 AND HB19CT1). FT VARIANT 128 128 D -> N (IN STRAINS 21343WI, 41552MA, HB19 FT AND HB19CT1). FT VARIANT 132 132 Q -> P (IN STRAIN CA8). FT VARIANT 176 176 A -> T (IN STRAIN CA8). FT VARIANT 189 189 S -> G (IN STRAIN CA8). FT VARIANT 192 192 L -> F (IN STRAIN CA8). FT VARIANT 198 198 V -> G (IN STRAINS 19535NY2, 27985CT2, FT 41552MA, 42373NY3, CA8, HB19 AND FT HB19CT1). FT VARIANT 218 218 K -> Q (IN STRAIN CA8). FT VARIANT 253 253 K -> T (IN STRAINS 21343WI, 41552MA, FT 42373NY3, HB19 AND HB19CT1). FT CONFLICT 12 12 A -> R (in Ref. 3). FT CONFLICT 214 214 R -> I (in Ref. 3). SQ SEQUENCE 296 AA; 31774 MW; 4A11D0AA6882310E CRC64; MRLLIGFALA LALIGCAQKG AESIGSQKEN DLNLEDSSKK SHQNAKQDLP AVTEDSVSLF NGNKIFVSKE KNSSGKYDLR ATIDQVELKG TSDKNNGSGT LEGSKPDKSK VKLTVSADLN TVTLEAFDAS NQKISSKVTK KQGSITEETL KANKLDSKKL TRSNGTTLEY SQITDADNAT KAVETLKNSI KLEGSLVVGK TTVEIKEGTV TLKREIEKDG KVKVFLNDTA GSNKKTGKWE DSTSTLTISA DSKKTKDLVF LTDGTITVQQ YNTAGTSLEG SASEIKNLSE LKNALK // ID OSMB_ECOLI STANDARD; PRT; 72 AA. AC P17873; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Osmotically inducible lipoprotein B precursor. GN OSMB OR B1283 OR C1753 OR Z2523 OR ECS1856 OR SF1287 OR S1370. OS Escherichia coli, OS Escherichia coli O6, OS Escherichia coli O157:H7, and OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562, 217992, 83334, 623; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; RX MEDLINE=89123064; PubMed=2644204; RA Jung J.U., Gutierrez C., Villarejo M.R.; RT "Sequence of an osmotically inducible lipoprotein gene."; RL J. Bacteriol. 171:511-520(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12; RX MEDLINE=97251357; PubMed=9097039; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., RA Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., RA Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., RA Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., RA Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., RA Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O6:H1 / CFT073 / ATCC 700928; RX MEDLINE=22388234; PubMed=12471157; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O157:H7 / EDL933 / ATCC 700927; RX MEDLINE=21074935; PubMed=11206551; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O157:H7 / RIMD 0509952; RX MEDLINE=21156231; PubMed=11258796; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=2457T / ATCC 700930 / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- FUNCTION: PROVIDES RESISTANCE TO OSMOTIC STRESS. MAY BE IMPORTANT CC FOR STATIONARY-PHASE SURVIVAL. CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- INDUCTION: By elevated osmotic pressure in the growth medium. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22859; AAA24256.1; -. DR EMBL; AE000226; AAC74365.1; -. DR EMBL; D90766; BAA14837.1; -. DR EMBL; AE016760; AAN80219.1; -. DR EMBL; AE005378; AAG56530.1; -. DR EMBL; AP002556; BAB35279.1; -. DR EMBL; AE015155; AAN42899.1; -. DR EMBL; AE016982; AAP16783.1; -. DR PIR; A32255; LPECOB. DR PIR; F85758; F85758. DR PIR; H90860; H90860. DR EcoGene; EG10679; osmB. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 23 FT CHAIN 24 72 Osmotically inducible lipoprotein B. FT LIPID 24 24 N-palmitoyl cysteine (Probable). FT LIPID 24 24 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 72 AA; 6948 MW; 3C41F7B8E15DEA65 CRC64; MFVTSKKMTA AVLAITLAMS LSACSNWSKR DRNTAIGAGA GALGGAVLTD GSTLGTLGGA AVGGVIGHQV GK // ID OSME_ECOLI STANDARD; PRT; 112 AA. AC P23933; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Osmotically inducible lipoprotein E precursor (Activator of ntr-like DE gene). GN OSME OR ANR OR B1739 OR Z2769 OR ECS2445 OR SF1487 OR S1604. OS Escherichia coli, OS Escherichia coli O157:H7, and OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562, 83334, 623; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12; RA Kim S., Wulff D.L.; RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12; RX MEDLINE=96037798; PubMed=7565114; RA Gutierrez C., Gordia S., Bonassie S.; RT "Characterization of the osmotically inducible gene osmE of RT Escherichia coli K-12."; RL Mol. Microbiol. 16:553-563(1995). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=K12; RX MEDLINE=97251357; PubMed=9097039; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., RA Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., RA Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., RA Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., RA Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., RA Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O157:H7 / EDL933 / ATCC 700927; RX MEDLINE=21074935; PubMed=11206551; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=E.coli; STRAIN=O157:H7 / RIMD 0509952; RX MEDLINE=21156231; PubMed=11258796; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=S.flexneri; STRAIN=2457T / ATCC 700930 / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- INDUCTION: By elevated osmotic pressure in the growth medium. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60186; CAA42743.1; -. DR EMBL; X75957; CAA53570.1; -. DR EMBL; AE000269; AAC74809.1; -. DR EMBL; D90817; BAA15528.1; -. DR EMBL; D90818; BAA15534.1; -. DR EMBL; AE005397; AAG56725.1; -. DR EMBL; AP002558; BAB35868.1; -. DR EMBL; AE015172; AAN43079.1; -. DR EMBL; AE016983; AAP16972.1; -. DR PIR; A85783; A85783. DR PIR; E90934; E90934. DR PIR; I57918; I57918. DR EcoGene; EG10044; osmE. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR007450; SmpA_OmlA. DR Pfam; PF04355; SmpA_OmlA; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 20 Probable. FT CHAIN 21 112 Osmotically inducible lipoprotein E. FT LIPID 21 21 N-palmitoyl cysteine (Probable). FT LIPID 21 21 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 112 AA; 12021 MW; CEF42E0DD8077550 CRC64; MNKNMAGILS AAAVLTMLAG CTAYDRTKDQ FVQPVVKDVK KGMSRAQVAQ IAGKPSSEVS MIHARGTCQT YILGQRDGKA ETYFVALDDT GHVINSGYQT CAEYDTDPQA AK // ID OUTS_ERWCH STANDARD; PRT; 133 AA. AC Q01567; DT 01-JUL-1993 (Rel. 26, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE OutS lipoprotein precursor. GN OUTS. OS Erwinia chrysanthemi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=556; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=3937; RX MEDLINE=93086427; PubMed=1453958; RA Condemine G., Dorel C., Hugouvieux-Cotte-Pattat N., Robert-Baudouy J.; RT "Some of the out genes involved in the secretion of pectate lyases in RT Erwinia chrysanthemi are regulated by kdgR."; RL Mol. Microbiol. 6:3199-3211(1992). RN [2] RP REVISIONS. RA Condemine G.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: OUT PROTEINS ARE REQUIRED FOR THE TRANSLOCATION OF CC PECTATE LYASES AND CELLULASES ACROSS THE OUTER MEMBRANE. CC -!- SIMILARITY: TO K.PNEUMONIAE PULS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65265; CAA46372.1; -. DR PIR; S28011; S28011. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR005699; PulS_OutS. DR TIGRFAMs; TIGR01004; PulS_OutS; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Transport; Protein transport; Outer membrane; Lipoprotein; Signal; KW Palmitate. FT SIGNAL 1 20 Probable. FT CHAIN 21 133 OutS lipoprotein. FT LIPID 21 21 N-palmitoyl cysteine (Probable). FT LIPID 21 21 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 133 AA; 14334 MW; 5948CEAEA124E9CB CRC64; MHVSSLKVVL FGVCCLSLAA CQTPAPVKNT ASRSAASVPA NEQISQLASL VAASKYLRVQ CERSDLPDDG TILKTAVNVA VQKGWDTGRY QSLPQLSENL YQGLLKDGTP KATQCSSFNR TMTPFLDAMR TVR // ID P22_BORBU STANDARD; PRT; 194 AA. AC Q05903; Q45008; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Outer surface 22 kDa lipoprotein precursor (Antigen IPLA7). GN P22 OR BB0365. OS Borrelia burgdorferi (Lyme disease spirochete). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=139; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ZS7; RX MEDLINE=94011300; PubMed=8104894; RA Wallich R., Simon M.M., Hofmann H., Moter S.E., Schaible U.E., RA Kramer M.D.; RT "Molecular and immunological characterization of a novel polymorphic RT lipoprotein of Borrelia burgdorferi."; RL Infect. Immun. 61:4158-4166(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=N40; RX MEDLINE=94299817; PubMed=8027338; RA Lam T., Nguyen T., Fikrig E., Flavell R.; RT "A chromosomal Borrelia burgdorferi gene encodes a 22-kilodalton RT lipoprotein, P22, that is serologically recognized in Lyme disease."; RL J. Clin. Microbiol. 32:876-883(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 35210 / B31; RX MEDLINE=98065943; PubMed=9403685; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., RA Dougherty B., Tomb J.-F., Fleischmann R.D., Richardson D., RA Peterson J., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J., RA Utterback T., Watthey L., McDonald L., Artiach P., Bowman C., RA Garland S., Fujii C., Cotton M.D., Horst K., Roberts K., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X70826; CAA50156.1; -. DR EMBL; L22530; AAC36908.1; -. DR EMBL; AE001142; AAC66748.1; -. DR PIR; D70145; D70145. DR TIGR; BB0365; -. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Antigen; Complete proteome; KW Palmitate. FT SIGNAL 1 21 Probable. FT CHAIN 22 194 Outer surface 22 kDa lipoprotein. FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). FT CONFLICT 14 14 F -> L (in Ref. 2). FT CONFLICT 74 74 K -> E (in Ref. 2). FT CONFLICT 129 129 P -> S (in Ref. 2). SQ SEQUENCE 194 AA; 21866 MW; D42A7CE0E26811B6 CRC64; MYKNGFFKNY LSLFLIFLVI ACTSKDSSNE YVEEQEAENS SKPDDSKIDE HTIGHVFHAM GVVHSKKDRK SLGKNIKVFY FSEEDGHFQT IPSKENAKLI VYFYDNVYAG EAPISISGKE AFIFVGITPD FKKIINSNLH GAKSDLIGTF KDLNIKNSKL EITVDENNSD AKTFLESVNY IIDGVEKISP MLTN // ID PAL_HAEIN STANDARD; PRT; 153 AA. AC P10324; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Outer membrane protein P6 precursor (OMP P6) (15 kDa peptidoglycan- DE associated lipoprotein) (PC protein). GN PAL OR OMPP6 OR HI0381. OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=88115138; PubMed=2828309; RA Deich R.A., Metcalf B.J., Finn C.W., Farley J.E., Green B.A.; RT "Cloning of genes encoding a 15,000-dalton peptidoglycan-associated RT outer membrane lipoprotein and an antigenically related 15,000-dalton RT protein from Haemophilus influenzae."; RL J. Bacteriol. 170:489-498(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88085463; PubMed=3257200; RA Nelson M.B., Apicella M.A., Murphy T.F., Vankeulen H., Spotila L.D., RA Rekosh D.; RT "Cloning and sequencing of Haemophilus influenzae outer membrane RT protein P6."; RL Infect. Immun. 56:128-134(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Rd / KW20 / ATCC 51907; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G., Fitzhugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- SIMILARITY: Belongs to the ompA family. Pal subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19391; AAA24994.1; -. DR EMBL; M18878; AAA24940.1; -. DR EMBL; U32722; AAC22039.1; -. DR PIR; A28543; A28543. DR TIGR; HI0381; -. DR InterPro; IPR006664; Bac_OmpA. DR InterPro; IPR006665; OmpA/MotB. DR InterPro; IPR006690; OMPA_LIKE. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00691; OmpA; 1. DR PRINTS; PR01021; OMPADOMAIN. DR ProDom; PD000930; OmpA/MotB; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS01068; OMPA; 1. KW Outer membrane; Signal; Lipoprotein; Complete proteome; Palmitate. FT SIGNAL 1 19 FT CHAIN 20 153 Outer membrane protein P6. FT LIPID 20 20 N-palmitoyl cysteine. FT LIPID 20 20 S-diacylglycerol cysteine. FT DOMAIN 85 129 OMPA-LIKE. SQ SEQUENCE 153 AA; 16108 MW; 3DF358122EF17A11 CRC64; MNKFVKSLLV AGSVAALAAC SSSNNDAAGN GAAQTFGGYS VADLQQRYNT VYFGFDKYDI TGEYVQILDA HAAYLNATPA AKVLVEGNTD ERGTPEYNIA LGQRRADAVK GYLAGKGVDA GKLGTVSYGE EKPAVLGHDE AAYSKNRRAV LAY // ID PCP_HAEIN STANDARD; PRT; 155 AA. AC P10325; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Outer membrane lipoprotein pcp precursor (15 kDa lipoprotein) (PAL DE cross-reacting lipoprotein). GN PCP OR LPP OR HI1579. OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88115138; PubMed=2828309; RA Deich R.A., Metcalf B.J., Finn C.W., Farley J.E., Green B.A.; RT "Cloning of genes encoding a 15,000-dalton peptidoglycan-associated RT outer membrane lipoprotein and an antigenically related 15,000-dalton RT protein from Haemophilus influenzae."; RL J. Bacteriol. 170:489-498(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Rd / KW20 / ATCC 51907; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G., Fitzhugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- SIMILARITY: TO E.COLI AND S.TYPHIMURIUM SLYB AND TO CC Y.ENTEROCOLITICA PCP. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18877; AAA24938.1; -. DR EMBL; U32832; AAC23228.1; -. DR PIR; I64130; I64130. DR TIGR; HI1579; -. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 18 FT CHAIN 19 155 Outer membrane lipoprotein pcp. FT LIPID 19 19 N-palmitoyl cysteine. FT LIPID 19 19 S-diacylglycerol cysteine. FT CONFLICT 135 143 CSLVAEFVF -> VAGRRVRI (in Ref. 1). SQ SEQUENCE 155 AA; 15425 MW; D7880327FCF0C985 CRC64; MKKTNMALAL LVAFSVTGCA NTDIFSGDVY SASQAKEARS ITYGTIVSVR PVKIQADNQG VVGTLGGGAL GGIAGSTIGG GRGQAIAAVV GAIGGAIAGS KIEEKMSQVN GAELVIKKDD GQEIVVVQKA DSSFCSLVAE FVFVGGGSSL NVSVL // ID PMEB_ERWCH STANDARD; PRT; 433 AA. AC Q47474; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pectinesterase B precursor (EC 3.1.1.11) (Pectin methylesterase B) DE (PE B). GN PEMB. OS Erwinia chrysanthemi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pectobacterium. OX NCBI_TaxID=556; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=3937; RX MEDLINE=96228695; PubMed=8830237; RA Shevchik V.E., Condemine G., Hugouvieux-Cotte-Pattat N., RA Robert-Baudouy J.; RT "Characterization of pectin methylesterase B, an outer membrane RT lipoprotein of Erwinia chrysanthemi 3937."; RL Mol. Microbiol. 19:455-466(1996). CC -!- FUNCTION: PROBABLY INVOLVED IN THE DEGRADATION OF METHYLATED CC OLIGOGALACTURONIDES PRESENT IN THE PERIPLASM. CC -!- CATALYTIC ACTIVITY: Pectin + N H(2)O = N methanol + pectate. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- INDUCTION: By pectin. CC -!- SIMILARITY: Belongs to the pectinesterase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X84665; CAA59151.1; -. DR PIR; S70914; S70914. DR InterPro; IPR000070; Pectinesterase. DR Pfam; PF01095; Pectinesterase; 1. DR PROSITE; PS00800; PECTINESTERASE_1; 1. DR PROSITE; PS00503; PECTINESTERASE_2; 1. KW Hydrolase; Aspartyl esterase; Outer membrane; Lipoprotein; Signal; KW Palmitate. FT SIGNAL 1 21 FT CHAIN 22 433 Pectinesterase B. FT LIPID 22 22 N-palmitoyl cysteine. FT LIPID 22 22 S-diacylglycerol cysteine. FT ACT_SITE 259 259 By similarity. FT ACT_SITE 292 292 By similarity. SQ SEQUENCE 433 AA; 46793 MW; 4854AD25F7619B18 CRC64; MSLTHYSGLA AAVSMSLILT ACGGQTPNSA RFQPVFPGTV SRPVLSAQEA GRFTPQHYFA HGGEYAKPVA DGWTPTPIDT SRVTAAYVVG PRAGVAGATH TSIQQAVNAA LRQHPGQTRV YIKLLPGTYT GTVYVPEGAP PLTLFGAGDR PEQVVVSLAL DSMMSPADYR ARVNPHGQYQ PADPAWYMYN ACATKAGATI NTTCSAVMWS QSNDFQLKNL TVVNALLDTV DSGTHQAVAL RTDGESGATG KCPPAQPSDT FFVNTSDRQN SYVTDHYSRA YIKDSYIEGD VDYVFGRATA VFDRVRFHTV SSRGSKEAYV FAPDSIPSVK YGFLVINSQL TGDNGYRGAQ KAKLGRAWDQ GAKQTGYLPG KTANGQLVIR DSTIDSSYDL ANPWGAAATT DRPFKGNISP QRDLDDIHFN RLWEYNTQVL LHE // ID PULA_KLEPN STANDARD; PRT; 1090 AA. AC P07206; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pullulanase precursor (EC 3.2.1.41) (Alpha-dextrin endo-1,6-alpha- DE glucosidase) (Pullulan 6-glucanohydrolase). GN PULA. OS Klebsiella pneumoniae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=573; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=UNF 5023; RX MEDLINE=90205629; PubMed=2181242; RA Kornacker M.G., Pugsley A.P.; RT "Molecular characterization of pulA and its product, pullulanase, a RT secreted enzyme of Klebsiella pneumoniae UNF5023."; RL Mol. Microbiol. 4:73-85(1990). RN [2] RP SEQUENCE OF 1-62 FROM N.A. RX MEDLINE=86033621; PubMed=3902792; RA Chapon C., Raibaud O.; RT "Structure of two divergent promoters located in front of the gene RT encoding pullulanase in Klebsiella pneumoniae and positively RT regulated by the malT product."; RL J. Bacteriol. 164:639-645(1985). RN [3] RP SEQUENCE OF 944-1090 FROM N.A. RX MEDLINE=89291709; PubMed=2661532; RA D'Enfert C., Pugsley A.P.; RT "Klebsiella pneumoniae pulS gene encodes an outer membrane RT lipoprotein required for pullulanase secretion."; RL J. Bacteriol. 171:3673-3679(1989). CC -!- CATALYTIC ACTIVITY: Hydrolysis of (1->6)-alpha-D-glucosidic CC linkages in pullulan and in amylopectin and glycogen, and the CC alpha- and beta-limit dextrins of amylopectin and glycogen. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- SIMILARITY: Belongs to family 13 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52181; CAA36431.1; -. DR EMBL; M12503; AAA25087.2; -. DR EMBL; M29097; AAA61976.1; -. DR PIR; S11823; S11823. DR InterPro; IPR006047; Alpha_amyl_cat. DR InterPro; IPR004193; Glyco_hydro_13N. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR005323; PUD. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02922; isoamylase_N; 1. DR Pfam; PF03714; PUD; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Hydrolase; Glycosidase; Membrane; Lipoprotein; Signal; Palmitate. FT SIGNAL 1 19 FT CHAIN 20 1090 Pullulanase. FT LIPID 20 20 N-palmitoyl cysteine. FT LIPID 20 20 S-diacylglycerol cysteine. FT ACT_SITE 684 684 By similarity. FT ACT_SITE 713 713 By similarity. FT ACT_SITE 841 841 By similarity. FT CONFLICT 6 6 R -> C (in Ref. 2). FT CONFLICT 10 10 V -> F (in Ref. 2). FT CONFLICT 15 15 V -> I (in Ref. 2). FT CONFLICT 23 23 G -> S (in Ref. 2). FT CONFLICT 31 31 N -> S (in Ref. 2). FT CONFLICT 34 34 T -> N (in Ref. 2). FT CONFLICT 36 36 D -> DGNP (in Ref. 2). FT CONFLICT 55 58 TAVE -> MATA (in Ref. 2). SQ SEQUENCE 1090 AA; 118098 MW; 240AE7DFB3FF1BD6 CRC64; MLRYTRNALV LGSLVLLSGC DNGSSSSSSG NPDTPDNQDV VVRLPDVAVP GEAVTAVENQ AVIHLVDIAG ITSSSAADYS SKNLYLWNNE TCDALSAPVA DWNDVSTTPS GSDKYGPYWV IPLNKESGCI NVIVRDGTDK LIDSDLRVAF GDFTDRTVSV IAGNSAVYDS RADAFRAAFG VALAEAHWVD KNTLLWPGGQ DKPIVRLYYS HSSKVAADGE GKFTDRYLKL TPTTVSQQVS MRFPHLSSYA AFKLPDNANV DELLQGETVA IAAAEDGILI SATQVQTAGV LDDAYAEAAE ALSYGAQLAD GGVTFRVWAP TAQQVDVVVY SADKKVIGSH PMTRDSASGA WSWQGGSDLK GAFYRYAMTV YHPQSRKVEQ YEVTDPYAHS LSTNSEYSQV VDLNDSALKP DGWDNLTMPH AQKTKADLAK MTIHESHIRD LSAWDQTVPA ELRGKYLALT AGDSNMVQHL KTLSASGVTH VELLPVFDLA TVNEFSDKVA DIQQPFSRLC EVNSAVKSSE FAGYCDSGST VEEVLNQLKQ SDSQDNPQVQ ALNTLVAQTD SYNWGYDPFH YTVPEGSYAT DPEGTTRIKE FRTMIQAIKQ DLGMNVIMDV VYNHTNAAGP TDRTSVLDKI VPWYYQRLNE TTGSVESATC CSDSAPEHRM FAKLIADSLA VWTTDYKIDG FRFDLMGYHP KAQILSAWER IKALNPDIYF FGEGWDSNQS DRFEIASQIN LKGTGIGTFS DRLRDSVRGG GPFDSGDALR QNQGIGSGAG VLPNELASLS DDQVRHLADL TRLGMAGNLA DFVMIDKDGA AKKGSEIDYN GAPGGYAADP TEVVNYVSKH DNQTLWDMIS YKASQEADLA TRVRMQAVSL ATVMLGQGIA FDQQGSELLR SKSFTRDSYD SGDWFNRVDY SLQDNNYNVG MPRISDDGSN YEVITRVKEM VATPGEAELK QMTAFYQELT ELRKSSPLFT LGDGSAVMKR VDFRNTGSDQ QAGLLVMTVD DGMKAGASLD SRLDGLVVAI NAAPESRTLN EFAGETLQLS AIQQTAGENS LANGVQIAAD GTVTLPAWSV AVLELPQGEA QGAGLPVSSK // ID PULS_KLEPN STANDARD; PRT; 125 AA. AC P20440; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pullulanase secretion protein pulS precursor. GN PULS. OS Klebsiella pneumoniae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=573; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89291709; PubMed=2661532; RA D'Enfert C., Pugsley A.P.; RT "Klebsiella pneumoniae pulS gene encodes an outer membrane RT lipoprotein required for pullulanase secretion."; RL J. Bacteriol. 171:3673-3679(1989). CC -!- FUNCTION: INVOLVED IN THE SECRETION OF PULLULANASE. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- SIMILARITY: TO E.CHRYSANTHEMI OUTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M29097; AAA61978.1; -. DR PIR; C32880; C32880. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR005699; PulS_OutS. DR TIGRFAMs; TIGR01004; PulS_OutS; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Transport; Protein transport; Outer membrane; Lipoprotein; Signal; KW Palmitate. FT SIGNAL 1 17 Probable. FT CHAIN 18 125 Pullulanase secretion protein pulS. FT LIPID 18 18 N-palmitoyl cysteine (Probable). FT LIPID 18 18 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 125 AA; 13808 MW; 450756F8FD98099D CRC64; MRNFILFPMM AVVLLSGCQQ NRPTTLSPAV SGQAQLEQLA SVAAGARYLK NKCNRSDLPA DEAINRAAIN VGKKRGWANI DANLLSQRSA QLYQQLQQDS TPEATKCSQF NRQLAPFIDS LRDNK // ID RLPA_ECOLI STANDARD; PRT; 362 AA. AC P10100; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Rare lipoprotein A precursor. GN RLPA OR B0633. OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE=88058785; PubMed=3316191; RA Takase I., Ishino F., Wachi M., Kamata H., Doi M., Asoh S., RA Matsuzawa H., Ohta T., Matsuhashi M.; RT "Genes encoding two lipoproteins in the leuS-dacA region of the RT Escherichia coli chromosome."; RL J. Bacteriol. 169:5692-5699(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [3] RP SEQUENCE FROM N.A. RA Chung E., Allen E., Araujo R., Aparicio A., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE=97061202; PubMed=8905232; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., RA Yano M., Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [5] RP SEQUENCE OF 1-16 FROM N.A. RC STRAIN=K12; RX MEDLINE=89123070; PubMed=2644207; RA Matsuzawa H., Asoh S., Kunai K., Muraiso K., Takasuga A., Ohta T.; RT "Nucleotide sequence of the rodA gene, responsible for the rod shape RT of Escherichia coli: rodA and the pbpA gene, encoding RT penicillin-binding protein 2, constitute the rodA operon."; RL J. Bacteriol. 171:558-560(1989). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- SIMILARITY: Belongs to the rlpA family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18276; AAA24552.1; -. DR EMBL; AE000168; AAC73734.1; -. DR EMBL; U82598; AAB40833.1; -. DR EMBL; D90703; BAA35276.1; -. DR EMBL; D90704; BAA35280.1; -. DR EMBL; M22857; AAA24572.1; -. DR PIR; A28387; LPECRA. DR ECO2DBASE; F037.4; 6TH EDITION. DR EcoGene; EG10854; rlpA. DR InterPro; IPR005132; Lipoprotein_13. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR007730; SPOR. DR Pfam; PF03330; Lipoprotein_13; 1. DR Pfam; PF05036; SPOR; 2. DR TIGRFAMs; TIGR00413; rlpA; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 17 FT CHAIN 18 362 Rare lipoprotein A. FT LIPID 18 18 N-palmitoyl cysteine. FT LIPID 18 18 S-diacylglycerol cysteine. SQ SEQUENCE 362 AA; 37528 MW; E28B57023CF15686 CRC64; MRKQWLGICI AAGMLAACTS DDGQQQTVSV PQPAVCNGPI VEISGADPRF EPLNATANQD YQRDGKSYKI VQDPSRFSQA GLAAIYDAEP GSNLTASGEA FDPTQLTAAH PTLPIPSYAR ITNLANGRMI VVRINDRGPY GNDRVISLSR AAADRLNTSN NTKVRIDPII VAQDGSLSGP GMACTTVAKQ TYALPAPPDL SGGAGTSSVS GPQGDILPVS NSTLKSEDPT GAPVTSSGFL GAPTTLAPGV LEGSEPTPAP QPVVTAPSTT PATSPAMVTP QAVSQSASGN FMVQVGAVSD QARAQQYQQQ LGQKFGVPGR VTQNGAVWRI QLGPFASKAE ASTLQQRLQT EAQLQSFITT AQ // ID RLPB_ECOLI STANDARD; PRT; 193 AA. AC P10101; P77576; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Rare lipoprotein B precursor. GN RLPB OR B0641 OR C0732. OS Escherichia coli, and OS Escherichia coli O6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562, 217992; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE=88058785; PubMed=3316191; RA Takase I., Ishino F., Wachi M., Kamata H., Doi M., Asoh S., RA Matsuzawa H., Ohta T., Matsuhashi M.; RT "Genes encoding two lipoproteins in the leuS-dacA region of the RT Escherichia coli chromosome."; RL J. Bacteriol. 169:5692-5699(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [3] RP SEQUENCE FROM N.A. RA Chung E., Allen E., Araujo R., Aparicio A., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE=97061202; PubMed=8905232; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., RA Yano M., Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [5] RP SEQUENCE FROM N.A. RC STRAIN=O6:H1 / CFT073 / ATCC 700928; RX MEDLINE=22388234; PubMed=12471157; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18277; AAA24554.1; -. DR EMBL; AE000168; AAC73742.1; -. DR EMBL; U82598; AAB40842.1; -. DR EMBL; D90704; BAA35288.1; -. DR EMBL; AE016757; AAN79205.1; -. DR PIR; G64798; LPECRB. DR EcoGene; EG10855; rlpB. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR007485; RplB. DR Pfam; PF04390; RplB; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 18 FT CHAIN 19 193 Rare lipoprotein B. FT LIPID 19 19 N-palmitoyl cysteine. FT LIPID 19 19 S-diacylglycerol cysteine. FT CONFLICT 117 117 P -> S (in Ref. 1). SQ SEQUENCE 193 AA; 21356 MW; C9387BC2008ADEDC CRC64; MRYLATLLLS LAVLITAGCG WHLRDTTQVP STMKVMILDS GDPNGPLSRA VRNQLRLNGV ELLDKETTRK DVPSLRLGKV SIAKDTASVF RNGQTAEYQM IMTVNATVLI PGRDIYPISA KVFRSFFDNP QMALAKDNEQ DMIVKEMYDR AAEQLIRKLP SIRAADIRSD EEQTSTTTDT PATPARVSTT LGN // ID SLP_ECOLI STANDARD; PRT; 188 AA. AC P37194; P76709; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Outer membrane protein slp precursor. GN SLP OR B3506. OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE=94293775; PubMed=8022277; RA Alexander D.M., St John A.C.; RT "Characterization of the carbon starvation-inducible and stationary RT phase-inducible gene slp encoding an outer membrane lipoprotein in RT Escherichia coli."; RL Mol. Microbiol. 11:1059-1071(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=94316500; PubMed=8041620; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the RT region from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). CC -!- FUNCTION: THE INDUCTION OF SLP MAY HELP TO STABILIZE THE OUTER CC MEMBRANE DURING CARBON STARVATION AND STATIONARY PHASE. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- INDUCTION: INDUCED UPON STARVATION AND SLOWED GROWTH. CAMP/CRP- CC INDEPENDENT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L23635; AAA60370.1; -. DR EMBL; U00039; AAB18482.1; ALT_INIT. DR EMBL; AE000427; AAC76531.1; ALT_INIT. DR PIR; S47726; S47726. DR EcoGene; EG11890; slp. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR004658; Slp. DR Pfam; PF03843; Slp; 1. DR TIGRFAMs; TIGR00752; slp; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Signal; Lipoprotein; Complete proteome; Palmitate. FT SIGNAL 1 18 FT CHAIN 19 188 Outer membrane protein slp. FT LIPID 19 19 N-palmitoyl cysteine. FT LIPID 19 19 S-diacylglycerol cysteine. SQ SEQUENCE 188 AA; 20964 MW; B2CDBC40E05ADB30 CRC64; MNMTKGALIL SLSFLLAACS SIPQNIKGNN QPDIQKSFVA VHNQPGLYVG QQARFGGKVI NVINGKTDTL LEISVLPLDS YAKPDIEANY QGRLLARQSG FLDPVNYRNH FVTILGTIQG EQPGFINKVP YNFLEVNMQG IQVWHLREVV NTTYNLWDYG YGAFWPEPGW GAPYYTNAVS QVTPELVK // ID SMPA_TREHY STANDARD; PRT; 159 AA. AC Q54313; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 16 kDa outer membrane lipoprotein precursor. GN SMPA. OS Treponema hyodysenteriae (Serpulina hyodysenteriae). OC Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=159; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=P18A; RX MEDLINE=93162807; PubMed=8432595; RA Thomas W., Sellwood R.; RT "Molecular cloning, expression, and DNA sequence analysis of the gene RT that encodes the 16-kilodalton outer membrane lipoprotein of RT Serpulina hyodysenteriae."; RL Infect. Immun. 61:1136-1140(1993). CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X68401; CAA48467.1; -. DR PIR; S33585; S33585. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Repeat; Outer membrane; Lipoprotein; Signal; Palmitate. FT SIGNAL 1 21 Probable. FT CHAIN 22 159 16 kDa outer membrane lipoprotein. FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 159 AA; 16838 MW; EF8C976DE09F32AE CRC64; MNKKIFTLFL VVAASAIFAV SCNNKTTNPT SNSSEKKIVT EEDFKNAIEG LTYKTWAFTG KGKSFNFGSP ITVEATSGSD SLAGVEKGFG NALKSALAAK GIDTGNITFD KGGASSSDKT SVSFKFTPKA LGTSNFEEKL KSSVKEVEIK LTPKENWGA // ID TA15_TREPA STANDARD; PRT; 141 AA. AC P16055; O83201; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 15 kDa lipoprotein precursor (Major membrane immunogen). GN TPP15 OR TP0171. OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91125139; PubMed=2280688; RA Purcell B.K., Radolf J.D.; RT "Lipid modification of the 15 kilodalton major membrane immunogen of RT Treponema pallidum."; RL Mol. Microbiol. 4:1371-1379(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=97473495; PubMed=9332349; RA Hardham J.M., Stamm L.V., Porcella S.F., Frye J.G., Barnes N.Y., RA Howell J.K., Mueller S.L., Radolf J.D., Weinstock G.M., Norris S.J.; RT "Identification and transcriptional analysis of a Treponema pallidum RT operon encoding a putative ABC transport system, an iron-activated RT repressor protein homolog, and a glycolytic pathway enzyme homolog."; RL Gene 197:47-64(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R., Gwinn M., Hickey E.K., Clayton R., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S., Peterson J., RA Khalak H., Richardson D., Howell J.K., Chidambaram M., Utterback T., RA McDonald L., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S., RA Hatch B., Horst K., Roberts K., Sandusky M., Weidman J., Smith H.O., RA Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U55214; AAC45732.1; -. DR EMBL; AE001201; AAC65160.1; -. DR TIGR; TP0171; -. DR InterPro; IPR007329; FMN_bind. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF04205; FMN_bind; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Antigen; Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 17 FT CHAIN 18 141 15 kDa lipoprotein. FT LIPID 18 18 N-palmitoyl cysteine (Probable). FT LIPID 18 18 S-diacylglycerol cysteine (Probable). FT CONFLICT 6 6 R -> GA (in Ref. 3). FT CONFLICT 124 124 R -> A (in Ref. 3). SQ SEQUENCE 141 AA; 15783 MW; BC00878646EADCF5 CRC64; MVKRGRFALC LAVLLGACSF SSIPNGTYRA TYQDFDENGW KDFLEVTFDG GKMVQVVYDY QHKEGRFKSQ DADYHRVMYA SSGIGPEKAF RELADALLEK GNPEMVDVVT GATVSSQSFR RLGRALLQSA RRGEKEAIIS R // ID TA17_TREPA STANDARD; PRT; 156 AA. AC P29722; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE 17 kDa lipoprotein precursor. GN TPP17 OR TP0435. OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93202716; PubMed=8454324; RA Akins D.R., Purcell B.K., Mitra M.M., Norgard M.V., Radolf J.D.; RT "Lipid modification of the 17-kilodalton membrane immunogen of RT Treponema pallidum determines macrophage activation as well as RT amphiphilicity."; RL Infect. Immun. 61:1202-1210(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R., Gwinn M., Hickey E.K., Clayton R., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S., Peterson J., RA Khalak H., Richardson D., Howell J.K., Chidambaram M., Utterback T., RA McDonald L., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S., RA Hatch B., Horst K., Roberts K., Sandusky M., Weidman J., Smith H.O., RA Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M74825; AAA27472.1; -. DR EMBL; AE001221; AAC65423.1; -. DR PIR; C71323; C71323. DR TIGR; TP0435; -. DR InterPro; IPR007298; NlpE. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF04170; NlpE; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; FALSE_NEG. KW Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 21 FT CHAIN 22 156 17 kDa lipoprotein. FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 156 AA; 16467 MW; 03630A2AACEA13F7 CRC64; MKGSVRALCA FLGVGALGSA LCVSCTTVCP HAGKAKAEKV ECALKGGIFR GTLPAADCPG IDTTVTFNAD GTAQKVELAL EKKSAPSPLT YRGTWMVRED GIVELSLVSS EQSKAPHEKE LYELIDSNSV RYMGAPGAGK PSKEMAPFYV LKKTKK // ID TA47_TREPA STANDARD; PRT; 434 AA. AC P29723; O83584; DT 01-APR-1993 (Rel. 25, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE 47 kDa membrane antigen precursor. GN TP0574. OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=Nichols; RX MEDLINE=92192832; PubMed=1372297; RA Weigel L.M., Brandt M.E., Norgard M.V.; RT "Analysis of the N-terminal region of the 47-kilodalton integral RT membrane lipoprotein of Treponema pallidum."; RL Infect. Immun. 60:1568-1576(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R., Gwinn M., Hickey E.K., Clayton R., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S., Peterson J., RA Khalak H., Richardson D., Howell J.K., Chidambaram M., Utterback T., RA McDonald L., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S., RA Hatch B., Horst K., Roberts K., Sandusky M., Weidman J., Smith H.O., RA Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). RN [3] RP SEQUENCE OF 68-434 FROM N.A. RC STRAIN=Nichols; RX MEDLINE=89079287; PubMed=2642466; RA Hsu P.L., Chamberlain N.R., Orth K., Moomaw C.R., Zhang L.Q., RA Slaughter C.A., Radolf J.D., Sell S., Norgard M.V.; RT "Sequence analysis of the 47-kilodalton major integral membrane RT immunogen of Treponema pallidum."; RL Infect. Immun. 57:196-203(1989). CC -!- FUNCTION: THIS ANTIGEN IS A PATHOGEN-SPECIFIC MEMBRANE IMMUNOGEN. CC MOST ABUNDANT OF THE MEMBRANE LIPOPROTEINS, ONLY FOUND SO FAR IN CC PATHOGENIC TREPONEMES, SUGGESTING THAT IT IS AN IMPORTANT CC STRUCTURAL MOIETY IN THE CELL ENVELOPE OF VIRULENT TREPONEMAL CC SUBSPECIES. CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M88769; AAA75016.1; -. DR EMBL; M88769; AAA75017.1; ALT_TERM. DR EMBL; AE001232; AAC65545.1; -. DR PIR; D71309; D71309. DR PDB; 1O75; 01-NOV-02. DR TIGR; TP0574; -. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Antigen; Membrane; Lipoprotein; Signal; Complete proteome; KW 3D-structure; Palmitate. FT SIGNAL 1 19 FT CHAIN 20 434 47 kDa membrane antigen. FT LIPID 20 20 N-palmitoyl cysteine (Probable). FT LIPID 20 20 S-diacylglycerol cysteine (Probable). FT CONFLICT 239 239 G -> V (in Ref. 1). FT STRAND 27 35 FT HELIX 36 44 FT TURN 45 45 FT TURN 48 48 FT HELIX 49 51 FT STRAND 72 75 FT HELIX 79 84 FT TURN 85 87 FT STRAND 88 104 FT TURN 106 107 FT STRAND 110 126 FT STRAND 128 133 FT TURN 135 136 FT STRAND 139 143 FT TURN 145 146 FT STRAND 148 148 FT TURN 152 153 FT STRAND 156 159 FT TURN 160 161 FT STRAND 162 182 FT HELIX 183 185 FT HELIX 186 193 FT STRAND 196 197 FT TURN 199 200 FT TURN 203 204 FT TURN 206 207 FT STRAND 208 213 FT TURN 214 215 FT STRAND 216 217 FT STRAND 221 221 FT TURN 228 229 FT STRAND 231 237 FT TURN 244 245 FT STRAND 248 256 FT TURN 257 258 FT HELIX 264 271 FT TURN 272 273 FT STRAND 274 281 FT TURN 283 284 FT TURN 286 287 FT STRAND 293 295 FT STRAND 299 299 FT TURN 300 302 FT STRAND 303 304 FT STRAND 312 317 FT TURN 319 320 FT HELIX 322 324 FT TURN 325 326 FT STRAND 330 338 FT TURN 339 340 FT STRAND 344 350 FT STRAND 359 370 FT TURN 374 379 FT STRAND 380 386 FT TURN 387 388 FT STRAND 393 398 FT STRAND 401 409 FT TURN 411 412 FT STRAND 414 420 FT STRAND 427 432 SQ SEQUENCE 434 AA; 47665 MW; B5C2A75D4A8849E0 CRC64; MKVKYALLSA GALQLLVVGC GSSHHETHYG YATLSYADYW AGELGQSRDV LLAGNAEADR AGDLDAGMFD AVSRATHGHG AFRQQFQYAV EVLGEKVLSK QETEDSRGRK KWEYETDPSV TKMVRASASF QDLGEDGEIK FEAVEGAVAL ADRASSFMVD SEEYKITNVK VHGMKFVPVA VPHELKGIAK EKFHFVEDSR VTENTNGLKT MLTEDSFSAR KVSSMESPHD LVVDTVGTGY HSRFGSDAEA SVMLKRADGS ELSHREFIDY VMNFNTVRYD YYGDDASYTN LMASYGTKHS ADSWWKTGRV PRISCGINYG FDRFKGSGPG YYRLTLIANG YRDVVADVRF LPKYEGNIDI GLKGKVLTIG GADAETLMDA AVDVFADGQP KLVSDQAVSL GQNVLSADFT PGTEYTVEVR FKEFGSVRAK VVAQ // ID TBB1_NEIMB STANDARD; PRT; 711 AA. AC Q09057; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Transferrin-binding protein 2 precursor (TBP-2). GN TBPB OR TBP2. OS Neisseria meningitidis (serogroup B). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=491; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=CCUG 37608 / M982 / Serogroup B / Serotype 9; RX MEDLINE=93345825; PubMed=8344530; RA Legrain M., Mazarin V., Irwin S.W., Bouchon B., Quentin-Millet M.-J., RA Jacobs E., Schryvers A.B.; RT "Cloning and characterization of Neisseria meningitidis genes RT encoding the transferrin-binding proteins Tbp1 and Tbp2."; RL Gene 130:73-80(1993). CC -!- FUNCTION: Acts as a transferrin receptor and is required for CC transferrin utilization. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor (Probable). CC -!- INDUCTION: By iron starvation. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z15130; CAA78832.1; -. DR PIR; JN0820; JN0820. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR001677; Transferrin_bind. DR Pfam; PF01298; Lipoprotein_5; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; FALSE_NEG. KW Outer membrane; Receptor; Signal; Lipoprotein; Palmitate. FT SIGNAL 1 20 FT CHAIN 21 711 Transferrin-binding protein 2. FT LIPID 21 21 N-palmitoyl cysteine (Probable). FT LIPID 21 21 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 711 AA; 76928 MW; A152654C1F5BFD85 CRC64; MNNPLVNQAA MVLPVFLLSA CLGGGGSFDL DSVDTEAPRP APKYQDVSSE KPQAQKDQGG YGFAMRLKRR NWYPGAEESE VKLNESDWEA TGLPTKPKEL PKRQKSVIEK VETDGDSDIY SSPYLTPSNH QNGSAGNGVN QPKNQATGHE NFQYVYSGWF YKHAASEKDF SNKKIKSGDD GYIFYHGEKP SRQLPASGKV IYKGVWHFVT DTKKGQDFRE IIQPSKKQGD RYSGFSGDGS EEYSNKNEST LKDDHEGYGF TSNLEVDFGN KKLTGKLIRN NASLNNNTNN DKHTTQYYSL DAQITGNRFN GTATATDKKE NETKLHPFVS DSSSLSGGFF GPQGEELGFR FLSDDQKVAV VGSAKTKDKL ENGAAASGST GAAASGGAAG TSSENSKLTT VLDAVELTLN DKKIKNLDNF SNAAQLVVDG IMIPLLPKDS ESGNTQADKG KNGGTEFTRK FEHTPESDKK DAQAGTQTNG AQTASNTAGD TNGKTKTYEV EVCCSNLNYL KYGMLTRKNS KSAMQAGGNS SQADAKTEQV EQSMFLQGER TDEKEIPTDQ NVVYRGSWYG HIANGTSWSG NASDKEGGNR AEFTVNFADK KITGKLTAEN RQAQTFTIEG MIQGNGFEGT AKTAESGFDL DQKNTTRTPK AYITDAKVKG GFYGPKAEEL GGWFAYPGDK QTEKATATSS DGNSASSATV VFGAKRQQPV Q // ID TMPA_TREPA STANDARD; PRT; 345 AA. AC P07643; DT 01-APR-1988 (Rel. 07, Created) DT 01-APR-1988 (Rel. 07, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Treponemal membrane protein A precursor (Antigen tmpA) (Membrane DE protein A). GN TMPA OR TP0768. OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Nichols; RX MEDLINE=85207444; PubMed=3922944; RA Hansen E.B., Pedersen P.E., Schouls L.M., Severin E., RA van Embden J.D.A.; RT "Genetic characterization and partial sequence determination of a RT Treponema pallidum operon expressing two immunogenic membrane RT proteins in Escherichia coli."; RL J. Bacteriol. 162:1227-1237(1985). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R., Gwinn M., Hickey E.K., Clayton R., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S., Peterson J., RA Khalak H., Richardson D., Howell J.K., Chidambaram M., Utterback T., RA McDonald L., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S., RA Hatch B., Horst K., Roberts K., Sandusky M., Weidman J., Smith H.O., RA Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). RN [3] RP MUTAGENESIS OF CYS-22. RC STRAIN=Nichols; RX MEDLINE=91372962; PubMed=1894360; RA Schouls L.M., van der Heide H.G.J., van Embden J.D.A.; RT "Characterization of the 35-kilodalton Treponema pallidum subsp. RT pallidum recombinant lipoprotein TmpC and antibody response to RT lipidated and nonlipidated T. pallidum antigens."; RL Infect. Immun. 59:3536-3546(1991). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor. CC -!- SIMILARITY: TO TMPA OF T.PHAGEDENIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M10931; AAA27481.1; -. DR EMBL; AE001248; AAC65736.1; -. DR PIR; A24587; A24587. DR TIGR; TP0768; -. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; FALSE_NEG. KW Antigen; Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 21 FT CHAIN 22 345 Treponemal membrane protein A. FT LIPID 22 22 N-palmitoyl cysteine. FT LIPID 22 22 S-diacylglycerol cysteine. FT MUTAGEN 22 22 C->S: LOSS OF LIPID INCORPORATION AND FT CLEAVAGE AT ALTERNATIVE PROCESSING SITE. SQ SEQUENCE 345 AA; 37285 MW; 92CA2331761BEC94 CRC64; MNAHTLVYSG VALACAAMLG SCASGAKEEA EKKAAEQRAL LVESAHADRR LMEARIGAQE SGADTQHPEL FSQIQDVERQ STDAKIEGDL KKAAGVASEA ADKYEILRNR VEVADLQSKI QTHQLAQYDG DSANAAEESW KKALELYETD SAQCLQSTVE ALESYRKVAH EGFGRLLPDM KARAGAAKTD VGGLKVAVEL RPQLEEADSQ YQEAREAEEV NARAKAFSGY HRALEIYTEL GKVVRLKKTE AEKALQSAKT KQKASSDLAR SADKSAPLPE NAQGFSKEPI EVEPLPNDRL NTTQADESAP IPISDTSSPS RVQSRGVEDG GRSPKSSMNE EGASR // ID TMPA_TREPH STANDARD; PRT; 344 AA. AC P29721; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Treponemal membrane protein A precursor (Antigen tmpA) (Membrane DE protein A). GN TMPA. OS Treponema phagedenis. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=162; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Kazan 5; RX MEDLINE=91372983; PubMed=1894368; RA Yelton D.B., Limberger R.J., Curci K., Malinosky-Rummell F., RA Sliviensky L., Schouls L.M., van Embden J.D., Charon N.W.; RT "Treponema phagedenis encodes and expresses homologs of the Treponema RT pallidum TmpA and TmpB proteins."; RL Infect. Immun. 59:3685-3693(1991). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor. CC -!- SIMILARITY: TO TMPA OF T.PALLIDIUM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M58475; AAA27482.1; -. DR PIR; A43592; A43592. DR InterPro; IPR000437; Prok_lipoprot_S. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Antigen; Membrane; Lipoprotein; Signal; Palmitate. FT SIGNAL 1 21 Probable. FT CHAIN 22 344 Treponemal membrane protein A. FT LIPID 22 22 N-palmitoyl cysteine (Probable). FT LIPID 22 22 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 344 AA; 37715 MW; 474833CC19B942FD CRC64; MKLKSLVFSL SALFLVLGFT GCKSKAQAKA EQEAQERKAF MAENAKIEKR LMQAKNAATE AEANVYYPEK FAQIEDLEKQ SSEAKEQDDL KKANSLGSAA ADKYETLANK MKIANQRSKI EANKLAKYDE ESYRLGEEAE KKIDGLYKSD SVAALQTSNE SLMYYNKVID AGYKSLSQDA KKTADDAKAA LTAVKVAASL KPQQEEADGI YAKAEEAENS AQYEQSYGGY TSAAQAYNDL TQIIKAKRLE AQKAMQAAKT KQELSAKLAN EADKESPLPE NAEGFSKEPI EVEPLPTDVL NAPQDEKAEE TVPVEEMNEN SSEEVNGNAE KIESTEEPIE GGVQ // ID TMPC_TREPA STANDARD; PRT; 353 AA. AC P29724; O83339; DT 01-APR-1993 (Rel. 25, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Membrane lipoprotein tmpC precursor (Membrane protein C) (35 kDa DE antigen) (Lipoprotein TpN35). GN TMPC OR TP0319. OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Nichols; RX MEDLINE=91372962; PubMed=1894360; RA Schouls L.M., van der Heide H.G.J., van Embden J.D.A.; RT "Characterization of the 35-kilodalton Treponema pallidum subsp. RT pallidum recombinant lipoprotein TmpC and antibody response to RT lipidated and nonlipidated T. pallidum antigens."; RL Infect. Immun. 59:3536-3546(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R., Gwinn M., Hickey E.K., Clayton R., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S., Peterson J., RA Khalak H., Richardson D., Howell J.K., Chidambaram M., Utterback T., RA McDonald L., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S., RA Hatch B., Horst K., Roberts K., Sandusky M., Weidman J., Smith H.O., RA Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). CC -!- SUBCELLULAR LOCATION: Attached to the membrane by a lipid anchor CC (Probable). CC -!- SIMILARITY: Belongs to the BMP lipoprotein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57836; CAA40968.1; -. DR EMBL; AE001211; AAC65302.1; -. DR PIR; H71340; H71340. DR TIGR; TP0319; -. DR InterPro; IPR003760; Bmp. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF02608; Bmp; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Antigen; Membrane; Lipoprotein; Signal; Complete proteome; Palmitate. FT SIGNAL 1 20 FT CHAIN 21 353 Membrane lipoprotein tmpC. FT LIPID 21 21 N-palmitoyl cysteine. FT LIPID 21 21 S-diacylglycerol cysteine. FT MUTAGEN 21 21 C->S: LOSS OF LIPID INCORPORATION AND FT CLEAVAGE AT ALTERNATIVE PROCESSING SITE. FT CONFLICT 11 11 G -> A (in Ref. 1). FT CONFLICT 159 159 A -> R (in Ref. 1). SQ SEQUENCE 353 AA; 37769 MW; CB373138C8C4337D CRC64; MREKWVRAFA GVFCAMLLIG CSKSDRPQMG NAGGAEGGDF VVGMVTDSGD IDDKSFNQQV WEGISRFAQE NNAKCKYVTA STDAEYVPSL SAFADENMGL VVACGSFLVE AVIETSARFP KQKFLVIDAV VQDRDNVVSA VFGQNEGSFL VGVAAALKAK EAGKSAVGFI VGMELGMMPL FEAGFEAGVK AVDPDIQVVV EVANTFSDPQ KGQALAAKLY DSGVNVIFQV AGGTGNGVIK EARDRRLNGQ DVWVIGVDRD QYMDGVYDGS KSVVLTSMVK RADVAAERIS KMAYDGSFPG GQSIMFGLED KAVGIPEENP NLSSAVMEKI RSFEEKIVSK EIVVPVRSAR MMN // ID TRT3_ECOLI STANDARD; PRT; 245 AA. AC P13980; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE TraT complement resistance protein precursor. GN TRAT. OS Escherichia coli. OG Plasmid IncFV pED208. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86223783; PubMed=3011738; RA Finlay B.B., Paranchych W.; RT "Nucleotide sequence of the surface exclusion genes traS and traT RT from the IncF0 lac plasmid pED208."; RL J. Bacteriol. 166:713-721(1986). CC -!- FUNCTION: Responsible for preventing unproductive conjugation CC between bacteria carrying like plasmids. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M13465; AAA88375.1; -. DR PIR; C29835; C29835. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR008874; TraT. DR Pfam; PF05818; TraT; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Plasmid; Conjugation; Signal; Lipoprotein; Outer membrane; Palmitate. FT SIGNAL 1 22 FT CHAIN 23 245 TraT complement resistance protein. FT LIPID 23 23 N-palmitoyl cysteine. FT LIPID 23 23 S-diacylglycerol cysteine. SQ SEQUENCE 245 AA; 25977 MW; 1DB93BA9E445B82A CRC64; MKHNVKLMAM TAVLSSVLVL SGCGAMSTAI KKRNLEVKTQ MSETIWLEPS SQKTVYLQIK NTSDKDMSGL QAKVTKAVQD KGYTITSSPD SAHYWIQANV LKADKMDLRT AQGFLSQGYE GAIAGAALGA GITGYNSSSA GATLGVGLAA GLVGMAADAM VEDINYTMVT DIQISEKTTA SVQTDNVAAL KQGTSGYKVQ TSTQTGNQHK YQTRIVSSAN KVNLKFEEAK PVLEDQLAKS VANIL // ID VACJ_SHIFL STANDARD; PRT; 251 AA. AC P43262; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE VacJ lipoprotein precursor. GN VACJ OR SF2424 OR S2559. OS Shigella flexneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=YSH6000 / Serotype 2a; RX MEDLINE=94195110; PubMed=8145644; RA Suzuki T., Murai T., Fukuda I., Tobe T., Yoshikawa M., Sasakawa C.; RT "Identification and characterization of a chromosomal virulence gene, RT vacJ, required for intercellular spreading of Shigella flexneri."; RL Mol. Microbiol. 11:31-41(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=301 / Serotype 2a; RX MEDLINE=22272406; PubMed=12384590; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., RA Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., RA Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., RA Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., RA Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=2457T / ATCC 700930 / Serotype 2a; RX MEDLINE=22590274; PubMed=12704152; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., RA Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., RA Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., RA Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella RT flexneri serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). CC -!- FUNCTION: REQUIRED FOR INTERCELLULAR SPREADING OF S.FLEXNERI. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D16293; BAA03799.1; -. DR EMBL; AE015258; AAN43935.1; -. DR EMBL; AE016986; AAP17748.1; -. DR InterPro; IPR000437; Prok_lipoprot_S. DR InterPro; IPR007428; VacJ. DR Pfam; PF04333; VacJ; 1. DR PRINTS; PR01805; VACJLIPOPROT. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Virulence; Outer membrane; Lipoprotein; Signal; Complete proteome; KW Palmitate. FT SIGNAL 1 17 FT CHAIN 18 251 VacJ lipoprotein. FT LIPID 18 18 N-palmitoyl cysteine. FT LIPID 18 18 S-diacylglycerol cysteine. SQ SEQUENCE 251 AA; 28021 MW; 3C6EC026191A3166 CRC64; MKLRLSALAL GTTLLVGCAS SGTDQQGRSD PLEGFNRTMY NFNFNVLDPY IVRPVAVAWR DYVPQPARNG LSNFTGNLEE PAVMVNYFLQ GDPYQGMVHF TRFFLNTILG MGGFIDVAGM ANPKLQRTEP HRFGSTLGHY GVGYGPYVQL PFYGSFTLRD DGGDMADALY PVLSWLTWPM SVGKWTLEGI ETRAQLLDSD GLLRQSSDPY IMVREAYFQR HDFIANGGEL KPQENPNAQA IQDDLKDIDS E // ID VM07_BORHE STANDARD; PRT; 369 AA. AC P21876; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Variable major outer membrane lipoprotein 7 precursor. GN VMP7. OS Borrelia hermsii. OG Plasmid. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=140; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Ssp. HS1 serotype 7; RX MEDLINE=91171872; PubMed=1706456; RA Burman N., Bergstroem S., Restrepo B.I., Barbour A.G.; RT "The variable antigens Vmp7 and Vmp21 of the relapsing fever RT bacterium Borrelia hermsii are structurally analogous to the VSG RT proteins of the African trypanosome."; RL Mol. Microbiol. 4:1715-1726(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Ssp. HS1 serotype 7; RX MEDLINE=93133110; PubMed=1484486; RA Restrepo B.I., Kitten T., Carter C.J., Infante D., Barbour A.G.; RT "Subtelomeric expression regions of Borrelia hermsii linear plasmids RT are highly polymorphic."; RL Mol. Microbiol. 6:3299-3311(1992). RN [3] RP SEQUENCE OF 52-72 AND 244-258. RX MEDLINE=85236116; PubMed=2409197; RA Barstad P.A., Coligan J.E., Raum M.G., Barbour A.G.; RT "Variable major proteins of Borrelia hermsii. Epitope mapping and RT partial sequence analysis of CNBr peptides."; RL J. Exp. Med. 161:1302-1314(1985). CC -!- FUNCTION: Serves to avoid the host immune response by changing CC from one surface exposed VMP to another. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- SIMILARITY: STRONG, TO VMP21 AND VMP25. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53926; CAA37873.1; -. DR EMBL; Z11876; CAA77935.1; -. DR PIR; S11980; S11980. DR InterPro; IPR000680; Borrelia_lipo. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00921; Lipoprotein_2; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Plasmid; Palmitate. FT SIGNAL 1 26 Probable. FT CHAIN 27 369 Variable major outer membrane lipoprotein FT 7. FT LIPID 27 27 N-palmitoyl cysteine (Probable). FT LIPID 27 27 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 369 AA; 37102 MW; F318727E39399DA8 CRC64; MRKRISAIIN KLNISIIIMT VVLMIGCGQQ PEAGKTGVSG GVNGNLGNSL MELGRSAENA FYAFIELVSD VLGFTAKSDT TKQEVGGYFN SLGAKLGEAS NDLEQVAVKA ETGVDKSDSS KNPIREAVNE AKEVLGTLKG YVESLGTIGD SNPVGYANNA AGSGTTAADD ELRKAFKALQ EIVKAATDAG VKALKIGATT LQANGGADNK EGAKILATSG GNPAAADVAK AAAILSSVSG EEMLSSIVKS GENDAQLAAA ADGNTSAISF AKGGSDAHLA GANTPKAAAV AGGIALRSLV KTGKLAAGAA DNATGGGKEV QGVGVAAANK LLRAVEDVIK KTVKNVLEKA KEKIDKARGS QEPVSESSK // ID VM17_BORHE STANDARD; PRT; 353 AA. AC P32777; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Variable major outer membrane lipoprotein 17 precursor. GN VMP17. OS Borrelia hermsii. OG Plasmid. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=140; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Ssp. HS1 serotype 17; RX MEDLINE=93133110; PubMed=1484486; RA Restrepo B.I., Kitten T., Carter C.J., Infante D., Barbour A.G.; RT "Subtelomeric expression regions of Borrelia hermsii linear plasmids RT are highly polymorphic."; RL Mol. Microbiol. 6:3299-3311(1992). CC -!- FUNCTION: Serves to avoid the host immune response by changing CC from one surface exposed VMP to another. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L04788; AAA22963.1; -. DR PIR; I40300; I40300. DR InterPro; IPR000680; Borrelia_lipo. DR InterPro; IPR001800; Lipoprotein_6. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00921; Lipoprotein_2; 1. DR Pfam; PF01441; Lipoprotein_6; 1. DR ProDom; PD001149; Lipoprotein_6; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Plasmid; Palmitate. FT SIGNAL 1 18 Probable. FT CHAIN 19 353 Variable major outer membrane lipoprotein FT 17. FT LIPID 19 19 N-palmitoyl cysteine (Probable). FT LIPID 19 19 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 353 AA; 36460 MW; 88FAB9B8C619AE91 CRC64; MRKRISAIIM TLFMVLVSCN SGGVAEDPKT VYLTSIANLG KGFLDVFVTF GDMVTGAFGI KADTKKSDIG KYFTDIESTM TSVKKKLQDE VAKNGNYPKV KTAVDEFVAI LGKIEKGAKE ASKGATGDVI IGNTVKNGDA VPGEATSVNS LVKGIKEIVG VVLKEGKADA DATKDDSKKD IGKLFTATTD ANRADNAAAQ AAAASIGAVT GADILQAIVQ SKENPVANST DGIEKATDAA EIAVAPAKDN KKEIKDGAKK DAVIAAGIAL RAMAKNGTFS IKNNEDAAVT TINSAAASAV NKILSTLIIA IRNTVDSGLK TINEALATVK QEDKSVEATN TAEATTSGQQ AKN // ID VM21_BORHE STANDARD; PRT; 364 AA. AC P21875; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Variable major outer membrane lipoprotein 21 precursor. GN VMP21. OS Borrelia hermsii. OG Plasmid. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia. OX NCBI_TaxID=140; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Ssp. HS1 serotype 21; RX MEDLINE=91171872; PubMed=1706456; RA Burman N., Bergstroem S., Restrepo B.I., Barbour A.G.; RT "The variable antigens Vmp7 and Vmp21 of the relapsing fever RT bacterium Borrelia hermsii are structurally analogous to the VSG RT proteins of the African trypanosome."; RL Mol. Microbiol. 4:1715-1726(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=Ssp. HS1 serotype 21; RX MEDLINE=93133110; PubMed=1484486; RA Restrepo B.I., Kitten T., Carter C.J., Infante D., Barbour A.G.; RT "Subtelomeric expression regions of Borrelia hermsii linear plasmids RT are highly polymorphic."; RL Mol. Microbiol. 6:3299-3311(1992). RN [3] RP SEQUENCE OF 55-75; 186-208 AND 245-259. RX MEDLINE=85236116; PubMed=2409197; RA Barstad P.A., Coligan J.E., Raum M.G., Barbour A.G.; RT "Variable major proteins of Borrelia hermsii. Epitope mapping and RT partial sequence analysis of CNBr peptides."; RL J. Exp. Med. 161:1302-1314(1985). CC -!- FUNCTION: Serves to avoid the host immune response by changing CC from one surface exposed VMP to another. CC -!- SUBCELLULAR LOCATION: Attached to the outer membrane by a lipid CC anchor. CC -!- SIMILARITY: STRONG, TO VMP7 AND VMP25. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M57256; AAB59031.1; -. DR PIR; S11981; S11981. DR InterPro; IPR000680; Borrelia_lipo. DR InterPro; IPR000437; Prok_lipoprot_S. DR Pfam; PF00921; Lipoprotein_2; 1. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Signal; Plasmid; Palmitate. FT SIGNAL 1 26 Probable. FT CHAIN 27 364 Variable major outer membrane lipoprotein FT 21. FT LIPID 27 27 N-palmitoyl cysteine (Probable). FT LIPID 27 27 S-diacylglycerol cysteine (Probable). SQ SEQUENCE 364 AA; 37084 MW; 16598B639EE63776 CRC64; MRKRISAIIN KLNISIMMMI VVLMIGCGQQ PEAGKTGAAG GEKQGAGSLS EVLMEVGKSA ENAFYSFLEL VSDTLGFTAK STTKKEDVGG YFNSLGGKLG EASNELEQVA KNSEAGIEKN DASKNPIRSA VNAAKKTLEA LKGYLDSLGT VGDSNPVGWA SNNAQGAAVD EAELKKAYKA LKGIMDTAEG AGVARPEVGN IAVKVGNGTD NKDGAKILAT DGAAAVGDAG KAAAILTTVS GKEMLASIVN STEDKAVKIT GNVTVETTPL EFAVGGNGAH LSQNANSKAA AVAGGIALRS LVKGGKLAAD NNDDDKASQG VGITAANKLL VAVEDIIKKT VKNVLEKAKG EIDKARDPKP AGQQ //