ID   SBI_STAA8               Reviewed;         436 AA.
AC   Q2FVK5; O52187; Q9R5V4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Immunoglobulin-binding protein Sbi;
DE   Flags: Precursor;
GN   Name=sbi; OrderedLocusNames=SAOUHSC_02706;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH IMMUNOGLOBULIN G.
RX   PubMed=9579072; DOI=10.1099/00221287-144-4-985;
RA   Zhang L., Jacobsson K., Vasi J., Lindberg M., Frykberg L.;
RT   "A second IgG-binding protein in Staphylococcus aureus.";
RL   Microbiology 144:985-991(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-121.
RX   PubMed=7619494;
RA   Jacobsson K., Frykberg L.;
RT   "Cloning of ligand-binding domains of bacterial receptors by phage
RT   display.";
RL   BioTechniques 18:878-885(1995).
RN   [4]
RP   INTERACTION WITH APOH, AND SUBCELLULAR LOCATION.
RX   PubMed=10206697; DOI=10.1099/13500872-145-1-177;
RA   Zhang L., Jacobsson K., Stroem K., Lindberg M., Frykberg L.;
RT   "Staphylococcus aureus expresses a cell surface protein that binds both IgG
RT   and beta-2-glycoprotein I.";
RL   Microbiology 145:177-183(1999).
RN   [5]
RP   INDUCTION BY IMMUNOGLOBULIN G, AND DEVELOPMENTAL STAGE.
RX   PubMed=10865173; DOI=10.1111/j.1574-695x.2000.tb01479.x;
RA   Zhang L., Rosander A., Jacobsson K., Lindberg M., Frykberg L.;
RT   "Expression of staphylococcal protein Sbi is induced by human IgG.";
RL   FEMS Immunol. Med. Microbiol. 28:211-218(2000).
RN   [6]
RP   SUBCELLULAR LOCATION, AND EXPORT MECHANISM.
RC   STRAIN=RN4220, and SH1000;
RX   PubMed=20472795; DOI=10.1128/jb.01452-09;
RA   Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA   Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA   van Dijl J.M.;
RT   "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT   Staphylococcus aureus.";
RL   J. Bacteriol. 192:3788-3800(2010).
CC   -!- FUNCTION: Plays a role in the inhibition of both the innate and
CC       adaptive immune responses. Possesses two N-terminal domains that bind
CC       the Fc region of IgG and two domains that form a tripartite complex
CC       with complement factors C3b and CFH. By recruiting CFH and C3b, the
CC       secreted form acts as a potent complement inhibitor of the alternative
CC       pathway-mediated lysis. {ECO:0000250|UniProtKB:A6QJQ7}.
CC   -!- SUBUNIT: Interacts (via sbi-I and sbi-II domains) with the Fc region of
CC       mammalian immunoglobulin G (IgG) proteins (By similarity)
CC       (PubMed:9579072). Interacts (via sbi-III and sbi-IV domains) with host
CC       complement C3 (By similarity). Interacts (via sbi-III and sbi-IV
CC       domains) with host CFH (By similarity). Interacts (via sbi-IV domain)
CC       with beta-2-glycoprotein 1/APOH (PubMed:10206697).
CC       {ECO:0000250|UniProtKB:A6QJQ7, ECO:0000269|PubMed:10206697,
CC       ECO:0000269|PubMed:9579072}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10206697,
CC       ECO:0000269|PubMed:20472795}. Cell membrane
CC       {ECO:0000250|UniProtKB:A6QJQ7}. Note=Occurs both extracellularly and
CC       associated with the cytoplasmic membrane where only the domains I and
CC       II are exposed to the extracellular media (By similarity). Membrane
CC       association occurs via binding to lipoteichoic acid (By similarity).
CC       {ECO:0000250|UniProtKB:A6QJQ7}.
CC   -!- DEVELOPMENTAL STAGE: Expression peaks approximately 2 hours after the
CC       addition of human IgG. {ECO:0000269|PubMed:10865173}.
CC   -!- INDUCTION: Strongly expressed in the presence of human IgG.
CC       {ECO:0000269|PubMed:10865173}.
CC   -!- DOMAIN: Sbi-I and sbi-II domains provide protection only when anchored
CC       to the cell surface, whereas only the secreted sbi-III and sbi-IV
CC       domains are biologically active. {ECO:0000250|UniProtKB:A6QJQ7}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin-binding protein Sbi family.
CC       {ECO:0000305}.
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DR   EMBL; AF027155; AAC38446.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD31714.1; -; Genomic_DNA.
DR   RefSeq; WP_000792564.1; NZ_LS483365.1.
DR   RefSeq; YP_501168.1; NC_007795.1.
DR   AlphaFoldDB; Q2FVK5; -.
DR   SMR; Q2FVK5; -.
DR   STRING; 1280.SAXN108_2673; -.
DR   EnsemblBacteria; ABD31714; ABD31714; SAOUHSC_02706.
DR   GeneID; 3919725; -.
DR   KEGG; sao:SAOUHSC_02706; -.
DR   PATRIC; fig|93061.5.peg.2450; -.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_051343_0_0_9; -.
DR   OMA; NAHASEQ; -.
DR   PRO; PR:Q2FVK5; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1270; -; 1.
DR   InterPro; IPR009063; Ig/albumin-bd_sf.
DR   InterPro; IPR021657; IgG-binding_Sbi_dom_IV.
DR   InterPro; IPR003132; Protein_A_Ig-bd.
DR   InterPro; IPR041909; Sbi_C3_db_domIV.
DR   Pfam; PF02216; B; 2.
DR   Pfam; PF11621; Sbi-IV; 1.
DR   SUPFAM; SSF46997; SSF46997; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; IgG-binding protein; Membrane; Reference proteome; Repeat;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..436
FT                   /note="Immunoglobulin-binding protein Sbi"
FT                   /id="PRO_0000361894"
FT   REPEAT          43..94
FT                   /note="B 1"
FT   REPEAT          95..148
FT                   /note="B 2"
FT   REPEAT          267..271
FT                   /note="2-1"
FT   REPEAT          272..276
FT                   /note="2-2"
FT   REPEAT          277..281
FT                   /note="2-3"
FT   REPEAT          282..286
FT                   /note="2-4"
FT   REPEAT          287..291
FT                   /note="2-5"
FT   REPEAT          292..296
FT                   /note="2-6"
FT   REPEAT          297..301
FT                   /note="2-7"
FT   REPEAT          302..306
FT                   /note="2-8"
FT   REGION          42..94
FT                   /note="Sbi-D1"
FT   REGION          103..153
FT                   /note="Sbi-D2"
FT   REGION          154..195
FT                   /note="Sbi-D3"
FT   REGION          196..253
FT                   /note="Sbi-D4"
FT   REGION          267..306
FT                   /note="8 X 5 AA tandem repeat of P-[KQ]-[AISV]-[EKQ]-
FT                   [AKLSV]"
SQ   SEQUENCE   436 AA;  50070 MW;  6526AE719C6CD051 CRC64;
     MKNKYISKLL VGAATITLAT MISNGEAKAS ENTQQTSTKH QTTQNNYVTD QQKAFYQVLH
     LKGITEEQRN QYIKTLREHP ERAQEVFSES LKDSKNPDRR VAQQNAFYNV LKNDNLTEQE
     KNNYIAQIKE NPDRSQQVWV ESVQSSKAKE RQNIENADKA IKDFQDNKAP HDKSAAYEAN
     SKLPKDLRDK NNRFVEKVSI EKAIVRHDER VKSANDAISK LNEKDSIENR RLAQREVNKA
     PMDVKEHLQK QLDALVAQKD AEKKVAPKVE APQIQSPQIE KPKVESPKVE VPQIQSPKVE
     VPQSKLLGYY QSLKDSFNYG YKYLTDTYKS YKEKYDTAKY YYNTYYKYKG AIDQTVLTVL
     GSGSKSYIQP LKVDDKNGYL AKSYAQVRNY VTESINTGKV LYTFYQNPTL VKTAIKAQET
     ASSIKNTLSN LLSFWK