FBE_STAEP
ID FBE_STAEP Reviewed; 1092 AA.
AC O70022;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Fibrinogen-binding protein;
DE Flags: Precursor;
GN Name=fbe;
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=HB;
RX PubMed=9596732; DOI=10.1128/iai.66.6.2666-2673.1998;
RA Nilsson M., Frykberg L., Flock J.-I., Pei L., Lindberg M., Guss B.;
RT "A fibrinogen-binding protein of Staphylococcus epidermidis.";
RL Infect. Immun. 66:2666-2673(1998).
RN [2]
RP INTERACTION WITH THE BETA-CHAIN OF FIBRINOGEN.
RC STRAIN=HB;
RX PubMed=10456895; DOI=10.1128/iai.67.9.4525-4530.1999;
RA Pei L., Palma M., Nilsson M., Guss B., Flock J.-I.;
RT "Functional studies of a fibrinogen binding protein from Staphylococcus
RT epidermidis.";
RL Infect. Immun. 67:4525-4530(1999).
RN [3]
RP FUNCTION.
RC STRAIN=HB;
RX PubMed=11535794; DOI=10.1099/00221287-147-9-2545;
RA Hartford O., O'Brien L., Schofield K., Wells J., Foster T.J.;
RT "The fbe (sdrG) protein of Staphylococcus epidermidis HB promotes bacterial
RT adherence to fibrinogen.";
RL Microbiology 147:2545-2552(2001).
RN [4]
RP ROLE IN PATHOGENICITY.
RC STRAIN=HB;
RX PubMed=17387162; DOI=10.1128/iai.01741-06;
RA Guo B., Zhao X., Shi Y., Zhu D., Zhang Y.;
RT "Pathogenic implication of a fibrinogen-binding protein of Staphylococcus
RT epidermidis in a rat intravascular catheter-associated infection model.";
RL Infect. Immun. 75:2991-2995(2007).
CC -!- FUNCTION: Promotes bacterial attachment to both soluble and immobilized
CC forms of fibrinogen in a dose-dependent manner. This binding occurs
CC through the beta-chain of human fibrinogen. Could contribute to the
CC initiation of foreign-body infection by allowing bacteria to adhere to
CC biomaterial surfaces that have become coated with host proteins after
CC implantation. Is important in the pathogenesis of central venous
CC catheter (CVC)-associated infection model.
CC {ECO:0000269|PubMed:11535794, ECO:0000269|PubMed:17387162,
CC ECO:0000269|PubMed:9596732}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- MISCELLANEOUS: The addition of calcium stimulates the interaction
CC between fbe and fibrinogen, but this effect could be due to calcium
CC binding to fibrinogen rather than to fbe.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; Y17116; CAA76638.1; -; Genomic_DNA.
DR PIR; T30214; T30214.
DR AlphaFoldDB; O70022; -.
DR SMR; O70022; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.1280; -; 1.
DR InterPro; IPR011266; Adhesin_Fg-bd_dom_2.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR033764; Sdr_B.
DR InterPro; IPR041171; SDR_Ig.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF17210; SdrD_B; 2.
DR Pfam; PF10425; SdrG_C_C; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell wall; Metal-binding; Peptidoglycan-anchor; Repeat; Secreted;
KW Signal; Virulence.
FT SIGNAL 1..51
FT /evidence="ECO:0000255"
FT CHAIN 52..1056
FT /note="Fibrinogen-binding protein"
FT /id="PRO_0000294170"
FT PROPEP 1057..1092
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000294171"
FT DOMAIN 600..713
FT /note="CNA-B 1"
FT DOMAIN 714..824
FT /note="CNA-B 2"
FT REGION 50..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..599
FT /note="Ligand binding A region"
FT REGION 579..590
FT /note="Interaction with human fibrinogen"
FT REGION 780..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1053..1057
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 51..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..1039
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9KI13"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9KI13"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9KI13"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9KI13"
FT MOD_RES 1056
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1092 AA; 119293 MW; 6542BC39AAD8B984 CRC64;
MINKKNNLLT KKKPIANKSN KYAIRKFTVG TASIVIGATL LFGLGHNEAK AEENSVQDVK
DSNTDDELSD SNDQSSDEEK NDVINNNQSI NTDDNNQIIK KEETNNYDGI EKRSEDRTES
TTNVDENEAT FLQKTPQDNT HLTEEEVKES SSVESSNSSI DTAQQPSHTT INREESVQTS
DNVEDSHVSD FANSKIKESN TESGKEENTI EQPNKVKEDS TTSQPSGYTN IDEKISNQDE
LLNLPINEYE NKARPLSTTS AQPSIKRVTV NQLAAEQGSN VNHLIKVTDQ SITEGYDDSE
GVIKAHDAEN LIYDVTFEVD DKVKSGDTMT VDIDKNTVPS DLTDSFTIPK IKDNSGEIIA
TGTYDNKNKQ ITYTFTDYVD KYENIKAHLK LTSYIDKSKV PNNNTKLDVE YKTALSSVNK
TITVEYQRPN ENRTANLQSM FTNIDTKNHT VEQTIYINPL RYSAKETNVN ISGNGDEGST
IIDDSTIIKV YKVGDNQNLP DSNRIYDYSE YEDVTNDDYA QLGNNNDVNI NFGNIDSPYI
IKVISKYDPN KDDYTTIQQT VTMQTTINEY TGEFRTASYD NTIAFSTSSG QGQGDLPPEK
TYKIGDYVWE DVDKDGIQNT NDNEKPLSNV LVTLTYPDGT SKSVRTDEDG KYQFDGLKNG
LTYKITFETP EGYTPTLKHS GTNPALDSEG NSVWVTINGQ DDMTIDSGFY QTPKYSLGNY
VWYDTNKDGI QGDDEKGISG VKVTLKDENG NIISTTTTDE NGKYQFDNLN SGNYIVHFDK
PSGMTQTTTD SGDDDEQDAD GEEVHVTITD HDDFSIDNGY YDDESDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SVSDSDSDSD
SDSGSDSDSD SDSDSDNDSD LGNSSDKSTK DKLPDTGANE DYGSKGTLLG TLFAGLGALL
LGKRRKNRKN KN
