SBI_STAAM
ID SBI_STAAM Reviewed; 426 AA.
AC Q931F4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Immunoglobulin-binding protein Sbi;
DE Flags: Precursor;
GN Name=sbi; OrderedLocusNames=SAV2418;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP INTERACTION WITH COMPONENT C3 AND IMMUNOGLOBULIN G, SUBCELLULAR LOCATION,
RP AND DOMAIN STRUCTURE.
RX PubMed=18434316; DOI=10.1074/jbc.m800265200;
RA Burman J.D., Leung E., Atkins K.L., O'Seaghdha M.N., Lango L., Bernado P.,
RA Bagby S., Svergun D.I., Foster T.J., Isenman D.E., van den Elsen J.M.H.;
RT "Interaction of human complement with Sbi, a staphylococcal immunoglobulin-
RT binding protein. Indications of a novel mechanism of complement evasion by
RT Staphylococcus aureus.";
RL J. Biol. Chem. 283:17579-17593(2008).
RN [3]
RP INTERACTION WITH THE FC REGION OF IMMUNOGLOBULIN G.
RX PubMed=18061675; DOI=10.1016/j.molimm.2007.10.021;
RA Atkins K.L., Burman J.D., Chamberlain E.S., Cooper J.E., Poutrel B.,
RA Bagby S., Jenkins A.T.A., Feil E.J., van den Elsen J.M.H.;
RT "S. aureus IgG-binding proteins SpA and Sbi: host specificity and
RT mechanisms of immune complex formation.";
RL Mol. Immunol. 45:1600-1611(2008).
RN [4] {ECO:0007744|PDB:2JVG, ECO:0007744|PDB:2JVH}
RP STRUCTURE BY NMR OF 198-266, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-231
RP AND ASN-238.
RX PubMed=18550524; DOI=10.1074/jbc.m802636200;
RA Upadhyay A., Burman J.D., Clark E.A., Leung E., Isenman D.E.,
RA van den Elsen J.M.H., Bagby S.;
RT "Structure-function analysis of the C3-binding region of Staphylococcus
RT aureus immune subversion protein Sbi.";
RL J. Biol. Chem. 283:22113-22120(2008).
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 ECO:0000269|PubMed:18550524}.
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. Interacts (via sbi-III and
CC sbi-IV domains) with host CFH (By similarity). Interacts (via sbi-IV
CC domain) with beta-2-glycoprotein 1/APOH (PubMed:18434316,
CC PubMed:18061675, PubMed:18550524). {ECO:0000250|UniProtKB:A6QJQ7,
CC ECO:0000269|PubMed:18061675, ECO:0000269|PubMed:18434316,
CC ECO:0000269|PubMed:18550524}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A6QJQ7}. Cell
CC membrane {ECO:0000250|UniProtKB:A6QJQ7}. Note=Occurs both
CC extracellularly and associated with the cytoplasmic membrane where only
CC the domains I and II are exposed to the extracellular media. Membrane
CC association occurs via binding to lipoteichoic acid.
CC {ECO:0000250|UniProtKB:A6QJQ7}.
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; BA000017; BAB58580.2; -; Genomic_DNA.
DR RefSeq; WP_000792562.1; NC_002758.2.
DR PDB; 2JVG; NMR; -; A=198-266.
DR PDB; 2JVH; NMR; -; A=198-266.
DR PDBsum; 2JVG; -.
DR PDBsum; 2JVH; -.
DR AlphaFoldDB; Q931F4; -.
DR SMR; Q931F4; -.
DR World-2DPAGE; 0002:Q931F4; -.
DR PaxDb; Q931F4; -.
DR EnsemblBacteria; BAB58580; BAB58580; SAV2418.
DR KEGG; sav:SAV2418; -.
DR HOGENOM; CLU_051343_0_0_9; -.
DR OMA; NAHASEQ; -.
DR BioCyc; SAUR158878:SAV_RS13175-MON; -.
DR EvolutionaryTrace; Q931F4; -.
DR PRO; PR:Q931F4; -.
DR Proteomes; UP000002481; 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 3D-structure; Cell membrane; IgG-binding protein; Membrane; Repeat;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..426
FT /note="Immunoglobulin-binding protein Sbi"
FT /id="PRO_0000361891"
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 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 266..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..296
FT /note="6 X 5 AA tandem repeat of P-[KQ]-[AISV]-[EKQ]-
FT [AKLSV]"
FT MUTAGEN 231
FT /note="R->A: Abolishes binding to complement component C3
FT derivatives and inhibition of the alternative pathway."
FT /evidence="ECO:0000269|PubMed:18550524"
FT MUTAGEN 238
FT /note="N->A: Abolishes binding to complement component C3
FT derivatives and inhibition of the alternative pathway."
FT /evidence="ECO:0000269|PubMed:18550524"
FT HELIX 202..223
FT /evidence="ECO:0007829|PDB:2JVG"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:2JVG"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2JVG"
FT HELIX 245..263
FT /evidence="ECO:0007829|PDB:2JVG"
SQ SEQUENCE 426 AA; 48936 MW; E61F85563B118AEE 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 KPKAESPKVE VPQSKLLGYY
QSLKDSFNYG YKYLTDTYKS YKEKYDTAKY YYNTYYKYKG AIDQTVLTVL GSGSKSYIQP
LKVDDKNGYL AKSYAQVRNY VTESINTGKV LYTFYQNPTL VKTAIKAQET ASSIKNTLSN
LLSFWK
