FIB_STAAN
ID FIB_STAAN Reviewed; 165 AA.
AC P68800; Q08691;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-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=SA1003;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42253.1; -; Genomic_DNA.
DR RefSeq; WP_000791581.1; NC_002745.2.
DR AlphaFoldDB; P68800; -.
DR SMR; P68800; -.
DR EnsemblBacteria; BAB42253; BAB42253; BAB42253.
DR KEGG; sau:SA1003; -.
DR HOGENOM; CLU_136810_0_0_9; -.
DR OMA; PRPHFNK; -.
DR PRO; PR:P68800; -.
DR Proteomes; UP000000751; 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 Secreted; Signal; Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..165
FT /note="Fibrinogen-binding protein"
FT /id="PRO_0000021259"
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