FIB_STAAE
ID FIB_STAAE Reviewed; 165 AA.
AC A6QG59; P68798; Q08691;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Fibrinogen-binding protein;
DE Flags: Precursor;
GN Name=fib; Synonyms=efb; OrderedLocusNames=NWMN_1069;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN FIBRINOGEN BINDING, AND
RP SUBCELLULAR LOCATION.
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [3]
RP PROTEIN SEQUENCE OF THE N-TERMINUS, AND BINDING TO FIBRINOGEN.
RX PubMed=1630299; DOI=10.1016/0882-4010(92)90047-r;
RA Boden M.K., Flock J.-I.;
RT "Evidence for three different fibrinogen-binding proteins with unique
RT properties from Staphylococcus aureus strain Newman.";
RL Microb. Pathog. 12:289-298(1992).
RN [4]
RP FUNCTION.
RC STRAIN=FDA486;
RX PubMed=8945578; DOI=10.1128/iai.64.12.5284-5289.1996;
RA Palma M., Nozohoor S., Schennings T., Heimdahl A., Flock J.I.;
RT "Lack of the extracellular 19-kilodalton fibrinogen-binding protein from
RT Staphylococcus aureus decreases virulence in experimental wound
RT infection.";
RL Infect. Immun. 64:5284-5289(1996).
RN [5]
RP INTERACTION WITH HOST FGA, AND FUNCTION.
RC STRAIN=Newman;
RX PubMed=11418620; DOI=10.1074/jbc.m104554200;
RA Palma M., Shannon O., Quezada H.C., Berg A., Flock J.I.;
RT "Extracellular fibrinogen-binding protein, Efb, from Staphylococcus aureus
RT blocks platelet aggregation due to its binding to the alpha-chain.";
RL J. Biol. Chem. 276:31691-31697(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH HOST C3 AND FGA.
RX PubMed=24348255; DOI=10.1371/journal.ppat.1003816;
RA Ko Y.P., Kuipers A., Freitag C.M., Jongerius I., Medina E.,
RA van Rooijen W.J., Spaan A.N., van Kessel K.P., Hoeoek M., Rooijakkers S.H.;
RT "Phagocytosis escape by a Staphylococcus aureus protein that connects
RT complement and coagulation proteins at the bacterial surface.";
RL PLoS Pathog. 9:E1003816-E1003816(2013).
RN [7]
RP FUNCTION.
RX PubMed=27112346; DOI=10.1099/mic.0.000293;
RA Kuipers A., Stapels D.A., Weerwind L.T., Ko Y.P., Ruyken M., Lee J.C.,
RA van Kessel K.P., Rooijakkers S.H.;
RT "The Staphylococcus aureus polysaccharide capsule and Efb-dependent
RT fibrinogen shield act in concert to protect against phagocytosis.";
RL Microbiology 162:1185-1194(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 101-164 IN COMPLEX WITH HOST C3,
RP AND MUTAGENESIS OF ARG-131 AND ASN-138.
RX PubMed=18687868; DOI=10.1110/ps.036624.108;
RA Haspel N., Ricklin D., Geisbrecht B.V., Kavraki L.E., Lambris J.D.;
RT "Electrostatic contributions drive the interaction between Staphylococcus
RT aureus protein Efb-C and its complement target C3d.";
RL Protein Sci. 17:1894-1906(2008).
CC -!- FUNCTION: Extracellular fibrinogen-binding protein that plays an
CC important role in virulence (PubMed:7934883, PubMed:8945578). By
CC interacting with the alpha chain of fibrinogen and its derivative
CC fibrin, enhances a non-functional interaction between fibrinogen and
CC platelets and is responsible for repression of fibrinogen-dependent
CC platelet aggregation (PubMed:11418620). In addition, assembles a
CC fibrinogen protective shield around the bacteria which results in
CC impaired phagocytic clearance by the host. Mechanistically, interacts
CC with host complement C3b deposited on the surface of the bacterium via
CC its C-terminal and then recruits fibrinogen via its N-terminal
CC (PubMed:24348255, PubMed:27112346). {ECO:0000269|PubMed:11418620,
CC ECO:0000269|PubMed:24348255, ECO:0000269|PubMed:27112346,
CC ECO:0000269|PubMed:7934883, ECO:0000269|PubMed:8945578}.
CC -!- SUBUNIT: Interacts with host fibrinogen alpha chain/FGA
CC (PubMed:11418620). Interacts with host complement protein C3
CC (PubMed:11418620, PubMed:24348255, PubMed:18687868).
CC {ECO:0000269|PubMed:11418620, ECO:0000269|PubMed:18687868,
CC ECO:0000269|PubMed:24348255}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; X72014; CAA50893.1; -; Genomic_DNA.
DR EMBL; AP009351; BAF67341.1; -; Genomic_DNA.
DR PIR; S49411; S34269.
DR PIR; S49413; S34270.
DR RefSeq; WP_000791587.1; NZ_CP023390.1.
DR PDB; 3D5R; X-ray; 2.10 A; C/D=101-164.
DR PDB; 3D5S; X-ray; 2.30 A; C/D=101-164.
DR PDBsum; 3D5R; -.
DR PDBsum; 3D5S; -.
DR AlphaFoldDB; A6QG59; -.
DR SMR; A6QG59; -.
DR EnsemblBacteria; BAF67341; BAF67341; NWMN_1069.
DR KEGG; sae:NWMN_1069; -.
DR HOGENOM; CLU_136810_0_0_9; -.
DR OMA; PRPHFNK; -.
DR EvolutionaryTrace; A6QG59; -.
DR PRO; PR:A6QG59; -.
DR Proteomes; UP000006386; 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; Direct protein sequencing; Secreted; Signal; Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..165
FT /note="Fibrinogen-binding protein"
FT /id="PRO_0000324754"
FT MUTAGEN 131
FT /note="R->A: Loss of host C3d binding stability."
FT /evidence="ECO:0000269|PubMed:18687868"
FT MUTAGEN 138
FT /note="N->A: Loss of host C3d binding stability."
FT /evidence="ECO:0000269|PubMed:18687868"
FT CONFLICT 4
FT /note="K -> A (in Ref. 1; CAA50893)"
FT /evidence="ECO:0000305"
FT HELIX 102..124
FT /evidence="ECO:0007829|PDB:3D5R"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:3D5R"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3D5R"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:3D5R"
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
