ID   FIB_STAAM               Reviewed;         165 AA.
AC   P68799; Q08691;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Fibrinogen-binding protein;
DE   Flags: Precursor;
GN   Name=fib; Synonyms=efb; OrderedLocusNames=SAV1158;
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   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 105-165 AND OF 101-165 IN COMPLEX
RP   WITH C3D DOMAIN OF HUMAN COMPLEMENT C3 PROTEIN.
RX   PubMed=17351618; DOI=10.1038/ni1450;
RA   Hammel M., Sfyroera G., Ricklin D., Magotti P., Lambris J.D.,
RA   Geisbrecht B.V.;
RT   "A structural basis for complement inhibition by Staphylococcus aureus.";
RL   Nat. Immunol. 8:430-437(2007).
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; BA000017; BAB57320.1; -; Genomic_DNA.
DR   RefSeq; WP_000791581.1; NC_002758.2.
DR   PDB; 2GOM; X-ray; 1.25 A; A/B=105-165.
DR   PDB; 2GOX; X-ray; 2.20 A; B/D=101-165.
DR   PDBsum; 2GOM; -.
DR   PDBsum; 2GOX; -.
DR   AlphaFoldDB; P68799; -.
DR   SMR; P68799; -.
DR   PaxDb; P68799; -.
DR   EnsemblBacteria; BAB57320; BAB57320; SAV1158.
DR   KEGG; sav:SAV1158; -.
DR   HOGENOM; CLU_136810_0_0_9; -.
DR   OMA; PRPHFNK; -.
DR   BioCyc; SAUR158878:SAV_RS06235-MON; -.
DR   EvolutionaryTrace; P68799; -.
DR   PRO; PR:P68799; -.
DR   Proteomes; UP000002481; 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   1: Evidence at protein level;
KW   3D-structure; Secreted; Signal; Virulence.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..165
FT                   /note="Fibrinogen-binding protein"
FT                   /id="PRO_0000021258"
FT   HELIX           106..124
FT                   /evidence="ECO:0007829|PDB:2GOM"
FT   HELIX           127..139
FT                   /evidence="ECO:0007829|PDB:2GOM"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:2GOM"
FT   HELIX           145..161
FT                   /evidence="ECO:0007829|PDB:2GOM"
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