ID OSPA_BORBU Reviewed; 273 AA. AC P0CL66; P0C926; P14013; Q44882; Q44964; Q44967; Q44969; Q44971; Q57123; AC Q57272; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=Outer surface protein A {ECO:0000303|PubMed:2761388}; DE Flags: Precursor; GN Name=ospA {ECO:0000303|PubMed:2761388}; OrderedLocusNames=BB_A15; OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OS (Borrelia burgdorferi). OG Plasmid lp54. OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae; OC Borreliella. OX NCBI_TaxID=224326; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=2761388; DOI=10.1111/j.1365-2958.1989.tb00194.x; RA Bergstroem S., Bundoc V., Barbour A.G.; RT "Molecular analysis of linear plasmid-encoded major surface proteins, OspA RT and OspB, of the Lyme disease spirochaete Borrelia burgdorferi."; RL Mol. Microbiol. 3:479-486(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=KA, and PBre; RX PubMed=7500914; DOI=10.1007/bf00221390; RA Will G., Jauris-Heipke S., Schwab E., Busch U., Roessler D., Soutschek E., RA 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 major RT subgroups within the Borrelia garinii species."; RL Med. Microbiol. Immunol. 184:73-80(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=KA; RX PubMed=8234271; DOI=10.1073/pnas.90.21.10163; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31; RX PubMed=9403685; DOI=10.1038/37551; 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.J., Hickey E.K., Gwinn M.L., RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., RA Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."; RL Nature 390:580-586(1997). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-273. RC STRAIN=19535NY2, 21343WI, 27985CT2, 41552MA, 42373NY3, CA3, CA7, CA8, RC and HB19CT1; RX PubMed=8121286; DOI=10.1093/oxfordjournals.molbev.a040092; 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 [6] RP FUNCTION, SUBCELLULAR LOCATION, DIACYLGLYCEROL AT CYS-17, AND RP PALMITOYLATION AT CYS-17. RC STRAIN=TI1-EV; RX PubMed=10426995; DOI=10.1126/science.285.5428.732; RA Brightbill H.D., Libraty D.H., Krutzik S.R., Yang R.B., Belisle J.T., RA Bleharski J.R., Maitland M., Norgard M.V., Plevy S.E., Smale S.T., RA Brennan P.J., Bloom B.R., Godowski P.J., Modlin R.L.; RT "Host defense mechanisms triggered by microbial lipoproteins through Toll- RT like receptors."; RL Science 285:732-736(1999). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS). RX PubMed=9108020; DOI=10.1073/pnas.94.8.3584; 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 / DSM 4680 / CIP 102532 / B31; RX PubMed=11183781; DOI=10.1006/jmbi.2000.4119; RA Ding W., Huang X., Yang X., Dunn J.J., Luft B.J., Koide S., 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 -!- FUNCTION: Induces host (human and mouse) cytokine release by monocyte CC cell lines via TLR2 and CD14; nonlipidated protein does not stimulate CC host cells (PubMed:10426995). {ECO:0000269|PubMed:10426995}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:2761388}; CC Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, CC ECO:0000305|PubMed:10426995}. Cell surface CC {ECO:0000305|PubMed:2761388}. CC -!- SIMILARITY: Belongs to the OspA lipoprotein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X14407; CAA32579.1; -; Genomic_DNA. DR EMBL; X85739; CAA59742.1; -; Genomic_DNA. DR EMBL; X80182; CAA56467.1; -; Genomic_DNA. DR EMBL; X69606; CAA49314.1; -; Genomic_DNA. DR EMBL; AE000790; AAC66260.1; -; Genomic_DNA. DR EMBL; L23136; AAA22951.1; -; Genomic_DNA. DR EMBL; L23137; AAA22953.1; -; Genomic_DNA. DR EMBL; L23138; AAA20947.1; -; Genomic_DNA. DR EMBL; L23139; AAA20949.1; -; Genomic_DNA. DR EMBL; L23140; AAA20951.1; -; Genomic_DNA. DR EMBL; L23141; AAA20953.1; -; Genomic_DNA. DR EMBL; L23142; AAA20955.1; -; Genomic_DNA. DR EMBL; L23143; AAA20957.1; -; Genomic_DNA. DR EMBL; L23144; AAA20959.1; -; Genomic_DNA. DR PIR; F49209; F49209. DR PIR; G70208; G70208. DR PIR; I40265; I40265. DR PIR; S71529; S71529. DR RefSeq; NP_045688.1; NC_001857.2. DR RefSeq; WP_010890378.1; NC_001857.2. DR PDB; 1FJ1; X-ray; 2.68 A; E/F=18-273. DR PDB; 1OSP; X-ray; 1.95 A; O=18-273. DR PDB; 2AF5; X-ray; 2.50 A; A=27-273. DR PDB; 2FKG; X-ray; 2.40 A; A=27-273. DR PDB; 2FKJ; X-ray; 3.10 A; A/B/C=27-273. DR PDB; 2G8C; X-ray; 1.15 A; O=27-273. DR PDB; 2HKD; X-ray; 1.60 A; A=27-130, A=118-273. DR PDB; 2I5V; X-ray; 1.10 A; O=27-273. DR PDB; 2I5Z; X-ray; 1.20 A; O=27-273. DR PDB; 2OL6; X-ray; 1.60 A; O=27-273. DR PDB; 2OL7; X-ray; 1.35 A; A/B=27-273. DR PDB; 2OL8; X-ray; 1.90 A; O=27-273. DR PDB; 2OY1; X-ray; 1.86 A; O=27-273. DR PDB; 2OY5; X-ray; 1.80 A; O=27-273. DR PDB; 2OY7; X-ray; 1.55 A; A=27-273. DR PDB; 2OY8; X-ray; 2.00 A; A=27-273. DR PDB; 2OYB; X-ray; 1.30 A; O=27-273. DR PDB; 2PI3; X-ray; 1.40 A; O=27-273. DR PDB; 3AUM; X-ray; 1.60 A; O=27-273. DR PDB; 5B2A; X-ray; 1.60 A; O=27-273. DR PDB; 6ICS; X-ray; 1.40 A; O=27-273. DR PDB; 6IDC; X-ray; 2.01 A; A=27-273. DR PDB; 6IEI; X-ray; 2.40 A; A=27-273. DR PDB; 6IYS; X-ray; 3.00 A; O=27-273. DR PDB; 6J47; X-ray; 1.90 A; O=27-273. DR PDB; 6J48; X-ray; 1.20 A; O=27-273. DR PDB; 6J49; X-ray; 1.60 A; O=27-273. DR PDB; 6J5M; X-ray; 1.85 A; O=27-273. DR PDB; 6J5N; X-ray; 1.73 A; O=27-273. DR PDB; 6J5O; X-ray; 1.90 A; O=27-273. DR PDB; 6J5P; X-ray; 1.80 A; O=27-273. DR PDB; 6J5Q; X-ray; 1.80 A; O=27-273. DR PDB; 6J5R; X-ray; 1.85 A; O=27-273. DR PDB; 6J6B; X-ray; 1.90 A; O=27-273. DR PDB; 6J6C; X-ray; 1.60 A; O=27-273. DR PDB; 6J6D; X-ray; 1.90 A; O=27-273. DR PDB; 6J6E; X-ray; 1.50 A; O=27-273. DR PDB; 6KT1; X-ray; 1.43 A; O=28-273. DR PDB; 6KWJ; X-ray; 1.94 A; B=27-273. DR PDB; 6KWU; X-ray; 1.43 A; O=27-273. DR PDB; 6KWV; X-ray; 1.37 A; O=27-273. DR PDB; 6LJY; X-ray; 1.50 A; O=27-273. DR PDB; 7JWG; X-ray; 3.05 A; C/E=23-273. DR PDB; 7T25; X-ray; 2.25 A; C/E=18-273. DR PDBsum; 1FJ1; -. DR PDBsum; 1OSP; -. DR PDBsum; 2AF5; -. DR PDBsum; 2FKG; -. DR PDBsum; 2FKJ; -. DR PDBsum; 2G8C; -. DR PDBsum; 2HKD; -. DR PDBsum; 2I5V; -. DR PDBsum; 2I5Z; -. DR PDBsum; 2OL6; -. DR PDBsum; 2OL7; -. DR PDBsum; 2OL8; -. DR PDBsum; 2OY1; -. DR PDBsum; 2OY5; -. DR PDBsum; 2OY7; -. DR PDBsum; 2OY8; -. DR PDBsum; 2OYB; -. DR PDBsum; 2PI3; -. DR PDBsum; 3AUM; -. DR PDBsum; 5B2A; -. DR PDBsum; 6ICS; -. DR PDBsum; 6IDC; -. DR PDBsum; 6IEI; -. DR PDBsum; 6IYS; -. DR PDBsum; 6J47; -. DR PDBsum; 6J48; -. DR PDBsum; 6J49; -. DR PDBsum; 6J5M; -. DR PDBsum; 6J5N; -. DR PDBsum; 6J5O; -. DR PDBsum; 6J5P; -. DR PDBsum; 6J5Q; -. DR PDBsum; 6J5R; -. DR PDBsum; 6J6B; -. DR PDBsum; 6J6C; -. DR PDBsum; 6J6D; -. DR PDBsum; 6J6E; -. DR PDBsum; 6KT1; -. DR PDBsum; 6KWJ; -. DR PDBsum; 6KWU; -. DR PDBsum; 6KWV; -. DR PDBsum; 6LJY; -. DR PDBsum; 7JWG; -. DR PDBsum; 7T25; -. DR AlphaFoldDB; P0CL66; -. DR BMRB; P0CL66; -. DR SMR; P0CL66; -. DR ABCD; P0CL66; 3 sequenced antibodies. DR EnsemblBacteria; AAC66260; AAC66260; BB_A15. DR KEGG; bbu:BB_A15; -. DR PATRIC; fig|224326.49.peg.1532; -. DR HOGENOM; CLU_1014382_0_0_12; -. DR OrthoDB; 351940at2; -. DR EvolutionaryTrace; P0CL66; -. DR Proteomes; UP000001807; Plasmid lp54. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:CAFA. DR Gene3D; 3.90.930.1; -; 1. DR Gene3D; 2.40.128.160; C1 set domains (antibody constant domain-like); 1. DR InterPro; IPR001809; OM_lipoprot_Borrelia. DR InterPro; IPR023322; OM_lipoprot_dom_sf. DR Pfam; PF00820; Lipoprotein_1; 1. DR PRINTS; PR00968; OUTRSURFACE. DR SUPFAM; SSF51087; Outer surface protein; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate; KW Plasmid; Reference proteome; Signal. FT SIGNAL 1..16 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT CHAIN 17..273 FT /note="Outer surface protein A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT /id="PRO_0000018074" FT LIPID 17 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303, FT ECO:0000305|PubMed:10426995" FT LIPID 17 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303, FT ECO:0000305|PubMed:10426995" FT VARIANT 35 FT /note="P -> S (in strain: CA7)" FT VARIANT 39 FT /note="K -> N (in strain: PBre and 21343WI)" FT VARIANT 59 FT /note="D -> H (in strain: 42373NY3)" FT VARIANT 90 FT /note="I -> V (in strain: CA8)" FT VARIANT 114 FT /note="V -> A (in strain: PBre)" FT VARIANT 127 FT /note="N -> S (in strain: CA8)" FT VARIANT 132..133 FT /note="VS -> LP (in strain: CA8)" FT VARIANT 144 FT /note="R -> K (in strain: 21343WI)" FT VARIANT 149 FT /note="G -> E (in strain: PBre and 42373NY3)" FT VARIANT 164 FT /note="G -> S (in strain: PBre)" FT VARIANT 196 FT /note="E -> A (in strain: CA8 and 21343WI)" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:1OSP" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:2I5V" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 38..42 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:2OY7" FT STRAND 52..58 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 61..72 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 85..90 FT /evidence="ECO:0007829|PDB:2I5V" FT TURN 92..95 FT /evidence="ECO:0007829|PDB:6J5R" FT STRAND 97..102 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 108..115 FT /evidence="ECO:0007829|PDB:2I5V" FT TURN 117..119 FT /evidence="ECO:0007829|PDB:3AUM" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:2I5V" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:6IYS" FT STRAND 132..138 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 144..149 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:7T25" FT STRAND 156..162 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 165..171 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 173..182 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 185..192 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:2I5V" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 212..217 FT /evidence="ECO:0007829|PDB:2I5V" FT TURN 218..221 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 230..237 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 243..248 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:2I5V" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:2I5Z" FT HELIX 265..271 FT /evidence="ECO:0007829|PDB:2I5V" SQ SEQUENCE 273 AA; 29367 MW; B53FC01D92F6D431 CRC64; MKKYLLGIGL ILALIACKQN VSSLDEKNSV SVDLPGEMKV LVSKEKNKDG KYDLIATVDK LELKGTSDKN NGSGVLEGVK ADKSKVKLTI SDDLGQTTLE VFKEDGKTLV SKKVTSKDKS STEEKFNEKG EVSEKIITRA DGTRLEYTGI KSDGSGKAKE VLKGYVLEGT LTAEKTTLVV KEGTVTLSKN ISKSGEVSVE LNDTDSSAAT KKTAAWNSGT STLTITVNSK KTKDLVFTKE NTITVQQYDS NGTKLEGSAV EITKLDEIKN ALK //