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SBI_STAAE
ID   SBI_STAAE               Reviewed;         436 AA.
AC   A6QJQ7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Immunoglobulin-binding protein Sbi;
DE   Flags: Precursor;
GN   Name=sbi; OrderedLocusNames=NWMN_2317;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
RN   [2]
RP   FUNCTION, INTERACTION WITH HOST C3 AND CFH, AND SUBCELLULAR LOCATION.
RC   STRAIN=H591;
RX   PubMed=19112495; DOI=10.1371/journal.ppat.1000250;
RA   Haupt K., Reuter M., van den Elsen J., Burman J., Haelbich S., Richter J.,
RA   Skerka C., Zipfel P.F.;
RT   "The Staphylococcus aureus protein Sbi acts as a complement inhibitor and
RT   forms a tripartite complex with host complement Factor H and C3b.";
RL   PLoS Pathog. 4:E1000250-E1000250(2008).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21708997; DOI=10.1128/iai.05075-11;
RA   Smith E.J., Visai L., Kerrigan S.W., Speziale P., Foster T.J.;
RT   "The Sbi protein is a multifunctional immune evasion factor of
RT   Staphylococcus aureus.";
RL   Infect. Immun. 79:3801-3809(2011).
RN   [4]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=22256861; DOI=10.1111/j.1365-2958.2011.07966.x;
RA   Smith E.J., Corrigan R.M., van der Sluis T., Gruendling A., Speziale P.,
RA   Geoghegan J.A., Foster T.J.;
RT   "The immune evasion protein Sbi of Staphylococcus aureus occurs both
RT   extracellularly and anchored to the cell envelope by binding lipoteichoic
RT   acid.";
RL   Mol. Microbiol. 83:789-804(2012).
RN   [5]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=Newman;
RX   PubMed=24434550; DOI=10.1073/pnas.1317181111;
RA   Becker S., Frankel M.B., Schneewind O., Missiakas D.;
RT   "Release of protein A from the cell wall of Staphylococcus aureus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:1574-1579(2014).
CC   -!- FUNCTION: Plays a role in the inhibition of both the innate and
CC       adaptive immune responses (PubMed:21708997). Possesses two N-terminal
CC       domains that bind the Fc region of IgG and two domains that form a
CC       tripartite complex with complement factors C3b and CFH. By recruiting
CC       CFH and C3b, the secreted form acts as a potent complement inhibitor of
CC       the alternative pathway-mediated lysis (PubMed:22256861,
CC       PubMed:19112495). {ECO:0000269|PubMed:19112495,
CC       ECO:0000269|PubMed:21708997, ECO:0000269|PubMed:22256861}.
CC   -!- SUBUNIT: Interacts (via sbi-I and sbi-II domains) with the Fc region of
CC       mammalian immunoglobulin G (IgG) proteins. Interacts (via sbi-III and
CC       sbi-IV domains) with host complement C3 (PubMed:19112495). Interacts
CC       (via sbi-III and sbi-IV domains) with host CFH (PubMed:19112495).
CC       Interacts (via sbi-IV domain) with beta-2-glycoprotein 1/APOH (By
CC       similarity). {ECO:0000250|UniProtKB:Q931F4,
CC       ECO:0000269|PubMed:19112495}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19112495,
CC       ECO:0000269|PubMed:21708997, ECO:0000269|PubMed:22256861,
CC       ECO:0000269|PubMed:24434550}. Cell membrane
CC       {ECO:0000269|PubMed:21708997, ECO:0000269|PubMed:22256861}. Note=Occurs
CC       both extracellularly and associated with the cytoplasmic membrane where
CC       only the domains I and II are exposed to the extracellular media
CC       (PubMed:21708997, PubMed:22256861). Membrane association occurs via
CC       binding to lipoteichoic acid (PubMed:22256861).
CC       {ECO:0000269|PubMed:21708997, ECO:0000269|PubMed:22256861}.
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:0000269|PubMed:21708997}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin-binding protein Sbi family.
CC       {ECO:0000305}.
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DR   EMBL; AP009351; BAF68589.1; -; Genomic_DNA.
DR   RefSeq; WP_000792564.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QJQ7; -.
DR   SMR; A6QJQ7; -.
DR   EnsemblBacteria; BAF68589; BAF68589; NWMN_2317.
DR   KEGG; sae:NWMN_2317; -.
DR   HOGENOM; CLU_051343_0_0_9; -.
DR   OMA; NAHASEQ; -.
DR   PRO; PR:A6QJQ7; -.
DR   Proteomes; UP000006386; 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; Repeat; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..436
FT                   /note="Immunoglobulin-binding protein Sbi"
FT                   /id="PRO_0000361895"
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-I"
FT   REGION          103..153
FT                   /note="Sbi-II"
FT   REGION          154..195
FT                   /note="Sbi-III"
FT   REGION          196..253
FT                   /note="Sbi-IV"
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
 
 
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