OSPA_BORBU
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 25-MAY-2022, entry version 62.
DE RecName: Full=Outer surface protein A;
DE Flags: Precursor;
GN Name=ospA; OrderedLocusNames=BB_A15;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OG Plasmid lp54.
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; 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, and
RC 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; Lipid-anchor
CC {ECO:0000305|PubMed:10426995}.
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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 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 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 OMA; ALIACKQ; -.
DR EvolutionaryTrace; P0CL66; -.
DR Proteomes; UP000001807; Plasmid lp54.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:CAFA.
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; SSF51087; 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 CHAIN 17..273
FT /note="Outer surface protein A"
FT /id="PRO_0000018074"
FT LIPID 17
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:10426995"
FT LIPID 17
FT /note="S-diacylglycerol cysteine"
FT /evidence="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:1FJ1"
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
