ID   FIB_STAAR               Reviewed;         165 AA.
AC   Q6GHS9;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Fibrinogen-binding protein;
DE   Flags: Precursor;
GN   Name=fib; Synonyms=efb; OrderedLocusNames=SAR1130;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40133.1; -; Genomic_DNA.
DR   RefSeq; WP_000791575.1; NC_002952.2.
DR   AlphaFoldDB; Q6GHS9; -.
DR   SMR; Q6GHS9; -.
DR   KEGG; sar:SAR1130; -.
DR   HOGENOM; CLU_136810_0_0_9; -.
DR   OMA; PRPHFNK; -.
DR   OrthoDB; 1578797at2; -.
DR   PRO; PR:Q6GHS9; -.
DR   Proteomes; UP000000596; 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_0000021260"
SQ   SEQUENCE   165 AA;  18835 MW;  5060987A1F144DB1 CRC64;
     MKNKLIAKSL LAIAAIGITT TTIASTADAS EGYGPREKKP VSINHNIVEY NDGTFKYQSR
     PKFNTTPKYI KFRHDYNIVE YNDGTFEYGA RPQFNKPAAK TEATIKKEQK LIQAQNLVRE
     FEKTHTVSAH RKAQKAVNLV SFEYNVKKMI LQERIDQVLK QGLVR