ID   FIB_STAAU               Reviewed;         165 AA.
AC   P0C6P2; P68798; Q08691;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Fibrinogen-binding protein;
DE   Flags: Precursor;
GN   Name=fib; Synonyms=efb;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN FIBRINOGEN BINDING, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=FDA 486;
RX   PubMed=7934883; DOI=10.1111/j.1365-2958.1994.tb01046.x;
RA   Boden M.K., Flock J.-I.;
RT   "Cloning and characterization of a gene for a 19 kDa fibrinogen-binding
RT   protein from Staphylococcus aureus.";
RL   Mol. Microbiol. 12:599-606(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=4074;
RX   PubMed=12089659; DOI=10.1086/341081;
RA   Heilmann C., Herrmann M., Kehrel B.E., Peters G.;
RT   "Platelet-binding domains in 2 fibrinogen-binding proteins of
RT   Staphylococcus aureus identified by phage display.";
RL   J. Infect. Dis. 186:32-39(2002).
CC   -!- FUNCTION: Extracellular fibrinogen-binding protein that plays an
CC       important role in virulence (PubMed:7934883). By interacting with the
CC       alpha chain of fibrinogen and its derivative fibrin, enhances a non-
CC       functional interaction between fibrinogen and platelets and is
CC       responsible for repression of fibrinogen-dependent platelet
CC       aggregation. In addition, assembles a fibrinogen protective shield
CC       around the bacteria which results in impaired phagocytic clearance by
CC       the host. Mechanistically, interacts with host complement C3b deposited
CC       on the surface of the bacterium via its C-terminal and then recruits
CC       fibrinogen via its N-terminal (By similarity).
CC       {ECO:0000250|UniProtKB:A6QG59, ECO:0000269|PubMed:7934883}.
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:0000269|PubMed:7934883}.
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DR   EMBL; X72013; CAA50892.1; -; Genomic_DNA.
DR   EMBL; AJ306909; CAC84780.1; -; Genomic_DNA.
DR   PIR; S49411; S34269.
DR   PIR; S49413; S34270.
DR   RefSeq; WP_000791581.1; NZ_WYDB01000003.1.
DR   AlphaFoldDB; P0C6P2; -.
DR   SMR; P0C6P2; -.
DR   OMA; PRPHFNK; -.
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   1: Evidence at protein level;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..29
FT   CHAIN           30..165
FT                   /note="Fibrinogen-binding protein"
FT                   /id="PRO_0000021262"
SQ   SEQUENCE   165 AA;  18793 MW;  D885BF0138415D70 CRC64;
     MKNKLIAKSL LTIAAIGITT TTIASTADAS EGYGPREKKP VSINHNIVEY NDGTFKYQSR
     PKFNSTPKYI KFKHDYNILE FNDGTFEYGA RPQFNKPAAK TDATIKKEQK LIQAQNLVRE
     FEKTHTVSAH RKAQKAVNLV SFEYKVKKMV LQERIDNVLK QGLVR