ID   FIB_STAAC               Reviewed;         165 AA.
AC   Q5HGS6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Fibrinogen-binding protein;
DE   Flags: Precursor;
GN   Name=fib; Synonyms=efb; OrderedLocusNames=SACOL1168;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Extracellular fibrinogen-binding protein that plays an
CC       important role in virulence. By interacting with the alpha chain of
CC       fibrinogen and its derivative fibrin, enhances a non-functional
CC       interaction between fibrinogen and platelets and is responsible for
CC       repression of fibrinogen-dependent platelet aggregation. In addition,
CC       assembles a fibrinogen protective shield around the bacteria which
CC       results in impaired phagocytic clearance by the host. Mechanistically,
CC       interacts with host complement C3b deposited on the surface of the
CC       bacterium via its C-terminal and then recruits fibrinogen via its N-
CC       terminal. {ECO:0000250|UniProtKB:A6QG59}.
CC   -!- SUBUNIT: Interacts with host fibrinogen alpha chain/FGA. Interacts with
CC       host complement protein C3. {ECO:0000250|UniProtKB:A6QG59}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A6QG59}.
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DR   EMBL; CP000046; AAW36547.1; -; Genomic_DNA.
DR   RefSeq; WP_000791587.1; NC_002951.2.
DR   AlphaFoldDB; Q5HGS6; -.
DR   SMR; Q5HGS6; -.
DR   ABCD; Q5HGS6; 1 sequenced antibody.
DR   EnsemblBacteria; AAW36547; AAW36547; SACOL1168.
DR   KEGG; sac:SACOL1168; -.
DR   HOGENOM; CLU_136810_0_0_9; -.
DR   OMA; PRPHFNK; -.
DR   PRO; PR:Q5HGS6; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0001848; F:complement binding; IEA:InterPro.
DR   Gene3D; 1.10.10.1270; -; 1.
DR   InterPro; IPR036233; Efb_C_sf.
DR   InterPro; IPR021033; Extracellular_fibrinogen-bd_C.
DR   InterPro; IPR041909; Sbi_C3_db_domIV.
DR   Pfam; PF12199; efb-c; 1.
DR   SUPFAM; SSF158366; SSF158366; 1.
PE   3: Inferred from homology;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..165
FT                   /note="Fibrinogen-binding protein"
FT                   /id="PRO_0000045203"
SQ   SEQUENCE   165 AA;  18765 MW;  BD929F216D415820 CRC64;
     MKNKLIAKSL LTLAAIGITT TTIASTADAS EGYGPREKKP VSINHNIVEY NDGTFKYQSR
     PKFNSTPKYI KFKHDYNILE FNDGTFEYGA RPQFNKPAAK TDATIKKEQK LIQAQNLVRE
     FEKTHTVSAH RKAQKAVNLV SFEYKVKKMV LQERIDNVLK QGLVK