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Database: UniProt
Entry: OSPA_BORBU
LinkDB: OSPA_BORBU
Original site: OSPA_BORBU 
ID   OSPA_BORBU              Reviewed;         273 AA.
AC   P0CL66; P0C926; P14013; Q44882; Q44964; Q44967; Q44969; Q44971;
AC   Q57123; Q57272;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   05-JUL-2017, entry version 36.
DE   RecName: Full=Outer surface protein A;
DE   Flags: Precursor;
GN   Name=ospA; OrderedLocusNames=BB_A15;
OS   Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM
OS   4680).
OG   Plasmid lp54.
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
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,
RT   OspA 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.,
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   [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 / B31 / CIP 102532 / DSM 4680;
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.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., 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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-273.
RC   STRAIN=19535NY2, 21343WI, 27985CT2, 41552MA, 42373NY3, CA3, CA7, CA8,
RC   and HB19CT1;
RX   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   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
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
RT   Toll-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 / B31 / CIP 102532 / DSM 4680;
RX   PubMed=11183781; DOI=10.1006/jmbi.2000.4119;
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   -!- FUNCTION: Induces host (human and mouse) cytokine release by
CC       monocyte cell lines via TLR2 and CD14; nonlipidated protein does
CC       not stimulate host cells (PubMed:10426995).
CC       {ECO:0000269|PubMed:10426995}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor
CC       {ECO:0000305|PubMed:10426995}.
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=27-130, A=119-273.
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; 5B10; X-ray; 1.60 A; O=27-273.
DR   PDB; 5B11; X-ray; 1.20 A; O=27-273.
DR   PDB; 5B2A; X-ray; 1.60 A; O=27-273.
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; 5B10; -.
DR   PDBsum; 5B11; -.
DR   PDBsum; 5B2A; -.
DR   SMR; P0CL66; -.
DR   PRIDE; P0CL66; -.
DR   EnsemblBacteria; AAC66260; AAC66260; BB_A15.
DR   GeneID; 1194357; -.
DR   KEGG; bbu:BB_A15; -.
DR   PATRIC; fig|224326.49.peg.1532; -.
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   GO; GO:0052157; P:modulation by symbiont of microbe-associated molecular pattern-induced host innate immune response; IDA:UniProtKB.
DR   Gene3D; 3.90.930.1; -; 1.
DR   InterPro; IPR001809; OM_lipoprot_Borrelia.
DR   InterPro; IPR023322; OM_lipoprot_dom.
DR   Pfam; PF00820; Lipoprotein_1; 1.
DR   PRINTS; PR00968; OUTRSURFACE.
DR   ProDom; PD001127; OM_lipoprot_Borrelia; 1.
DR   SUPFAM; SSF51087; SSF51087; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell outer membrane; Complete proteome; Lipoprotein;
KW   Membrane; Palmitate; Plasmid; Reference proteome; Signal.
FT   SIGNAL        1     16
FT   CHAIN        17    273       Outer surface protein A.
FT                                /FTId=PRO_0000018074.
FT   LIPID        17     17       N-palmitoyl cysteine.
FT                                {ECO:0000305|PubMed:10426995}.
FT   LIPID        17     17       S-diacylglycerol cysteine.
FT                                {ECO:0000305|PubMed:10426995}.
FT   VARIANT      35     35       P -> S (in strain: CA7).
FT   VARIANT      39     39       K -> N (in strain: PBre and 21343WI).
FT   VARIANT      59     59       D -> H (in strain: 42373NY3).
FT   VARIANT      90     90       I -> V (in strain: CA8).
FT   VARIANT     114    114       V -> A (in strain: PBre).
FT   VARIANT     127    127       N -> S (in strain: CA8).
FT   VARIANT     132    133       VS -> LP (in strain: CA8).
FT   VARIANT     144    144       R -> K (in strain: 21343WI).
FT   VARIANT     149    149       G -> E (in strain: PBre and 42373NY3).
FT   VARIANT     164    164       G -> S (in strain: PBre).
FT   VARIANT     196    196       E -> A (in strain: CA8 and 21343WI).
FT   HELIX        26     28       {ECO:0000244|PDB:1OSP}.
FT   STRAND       30     34       {ECO:0000244|PDB:2I5V}.
FT   TURN         35     37       {ECO:0000244|PDB:2I5V}.
FT   STRAND       38     42       {ECO:0000244|PDB:2I5V}.
FT   STRAND       48     50       {ECO:0000244|PDB:2OY7}.
FT   STRAND       52     58       {ECO:0000244|PDB:2I5V}.
FT   STRAND       61     72       {ECO:0000244|PDB:2I5V}.
FT   STRAND       74     79       {ECO:0000244|PDB:2I5V}.
FT   STRAND       85     90       {ECO:0000244|PDB:2I5V}.
FT   STRAND       97    102       {ECO:0000244|PDB:2I5V}.
FT   STRAND      108    115       {ECO:0000244|PDB:2I5V}.
FT   TURN        117    119       {ECO:0000244|PDB:3AUM}.
FT   STRAND      121    126       {ECO:0000244|PDB:2I5V}.
FT   STRAND      132    138       {ECO:0000244|PDB:2I5V}.
FT   STRAND      144    149       {ECO:0000244|PDB:2I5V}.
FT   STRAND      152    154       {ECO:0000244|PDB:1FJ1}.
FT   STRAND      156    162       {ECO:0000244|PDB:2I5V}.
FT   STRAND      165    171       {ECO:0000244|PDB:2I5V}.
FT   STRAND      173    182       {ECO:0000244|PDB:2I5V}.
FT   STRAND      185    192       {ECO:0000244|PDB:2I5V}.
FT   STRAND      197    203       {ECO:0000244|PDB:2I5V}.
FT   TURN        208    210       {ECO:0000244|PDB:2I5V}.
FT   STRAND      212    217       {ECO:0000244|PDB:2I5V}.
FT   TURN        218    221       {ECO:0000244|PDB:2I5V}.
FT   STRAND      222    227       {ECO:0000244|PDB:2I5V}.
FT   STRAND      230    237       {ECO:0000244|PDB:2I5V}.
FT   STRAND      243    248       {ECO:0000244|PDB:2I5V}.
FT   STRAND      252    255       {ECO:0000244|PDB:2I5V}.
FT   STRAND      260    262       {ECO:0000244|PDB:2I5Z}.
FT   HELIX       265    271       {ECO:0000244|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
//
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