CLFB_STAA8
ID CLFB_STAA8 Reviewed; 877 AA.
AC Q2FUY2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Clumping factor B;
DE AltName: Full=Fibrinogen receptor B;
DE AltName: Full=Fibrinogen-binding protein B;
DE Flags: Precursor;
GN Name=clfB; OrderedLocusNames=SAOUHSC_02963;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP CLEAVAGE BY AUREOLYSIN.
RX PubMed=11399757; DOI=10.1074/jbc.m102389200;
RA McAleese F.M., Walsh E.J., Sieprawska M., Potempa J., Foster T.J.;
RT "Loss of clumping factor B fibrinogen binding activity by Staphylococcus
RT aureus involves cessation of transcription, shedding and cleavage by
RT metalloprotease.";
RL J. Biol. Chem. 276:29969-29978(2001).
RN [3]
RP FUNCTION.
RX PubMed=12427098; DOI=10.1046/j.1462-5822.2002.00231.x;
RA O'Brien L.M., Walsh E.J., Massey R.C., Peacock S.J., Foster T.J.;
RT "Staphylococcus aureus clumping factor B (ClfB) promotes adherence to human
RT type I cytokeratin 10: implications for nasal colonization.";
RL Cell. Microbiol. 4:759-770(2002).
RN [4]
RP FUNCTION.
RX PubMed=15385531; DOI=10.1074/jbc.m408713200;
RA Walsh E.J., O'Brien L.M., Liang X., Hoeoek M., Foster T.J.;
RT "Clumping factor B, a fibrinogen-binding MSCRAMM (microbial surface
RT components recognizing adhesive matrix molecules) adhesin of Staphylococcus
RT aureus, also binds to the tail region of type I cytokeratin 10.";
RL J. Biol. Chem. 279:50691-50699(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE A.
RC STRAIN=RN4220;
RX PubMed=11830639; DOI=10.1073/pnas.032523999;
RA Mazmanian S.K., Ton-That H., Su K., Schneewind O.;
RT "An iron-regulated sortase anchors a class of surface protein during
RT Staphylococcus aureus pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2293-2298(2002).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=RN4220;
RX PubMed=18800056; DOI=10.1038/emboj.2008.185;
RA DeDent A., Bae T., Missiakas D.M., Schneewind O.;
RT "Signal peptides direct surface proteins to two distinct envelope locations
RT of Staphylococcus aureus.";
RL EMBO J. 27:2656-2668(2008).
CC -!- FUNCTION: Cell surface-associated protein implicated in virulence by
CC promoting bacterial attachment to both alpha- and beta-chains of human
CC fibrinogen and inducing the formation of bacterial clumps. Partly
CC responsible for mediating bacterial attachment to the highly
CC keratinized squamous epithelial cells from the nasal cavity via an
CC interaction with cytokeratin K10 (K10). Also promotes bacterial
CC attachment to cultured keratinocytes, possibly through an interaction
CC with cytokeratin K10. Binds mouse cytokeratin K10. Activates human
CC platelet aggregation. {ECO:0000269|PubMed:12427098,
CC ECO:0000269|PubMed:15385531}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:18800056,
CC ECO:0000305|PubMed:11830639}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639}.
CC Note=Found in a ring-like distribution on the cell surface
CC (PubMed:18800056). Colocalizes with SdrD (PubMed:18800056). Anchored to
CC the cell wall by sortase A (Probable). {ECO:0000269|PubMed:18800056,
CC ECO:0000305|PubMed:11830639}.
CC -!- DOMAIN: The Asp/Ser-rich domain functions as a stalk to allow the
CC ligand binding domain to be displayed in a functional form on the cell
CC surface.
CC -!- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage leads
CC to the inactivation of ClfB. {ECO:0000269|PubMed:11399757}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; CP000253; ABD31953.1; -; Genomic_DNA.
DR RefSeq; WP_000745896.1; NZ_LS483365.1.
DR RefSeq; YP_501414.1; NC_007795.1.
DR AlphaFoldDB; Q2FUY2; -.
DR SMR; Q2FUY2; -.
DR STRING; 93061.SAOUHSC_02963; -.
DR EnsemblBacteria; ABD31953; ABD31953; SAOUHSC_02963.
DR GeneID; 3921665; -.
DR KEGG; sao:SAOUHSC_02963; -.
DR PATRIC; fig|93061.5.peg.2673; -.
DR eggNOG; COG2931; Bacteria.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_004137_2_0_9; -.
DR OMA; KPVHPSI; -.
DR PRO; PR:Q2FUY2; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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; IPR019931; LPXTG_anchor.
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; 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 Cell wall; Peptidoglycan-anchor; Reference proteome; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..841
FT /note="Clumping factor B"
FT /id="PRO_0000248950"
FT PROPEP 842..877
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:11830639"
FT /id="PRO_0000248951"
FT REGION 44..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..542
FT /note="Ligand binding A region"
FT REGION 530..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..26
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000305|PubMed:18800056"
FT MOTIF 272..276
FT /note="MIDAS-like motif"
FT MOTIF 838..842
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 544..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..798
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 197..198
FT /note="Cleavage; by aureolysin"
FT SITE 199..200
FT /note="Cleavage; by aureolysin"
FT MOD_RES 841
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 877 AA; 93595 MW; 964B37A6A63B8904 CRC64;
MKKRIDYLSN KQNKYSIRRF TVGTTSVIVG ATILFGIGNH QAQASEQSND TTQSSKNNAS
ADSEKNNMIE TPQLNTTAND TSDISANTNS ANVDSTTKPM STQTSNTTTT EPASTNETPQ
PTAIKNQATA AKMQDQTVPQ EANSQVDNKT TNDANSIATN SELKNSQTLD LPQSSPQTIS
NAQGTSKPSV RTRAVRSLAV AEPVVNAADA KGTNVNDKVT ASNFKLEKTT FDPNQSGNTF
MAANFTVTDK VKSGDYFTAK LPDSLTGNGD VDYSNSNNTM PIADIKSTNG DVVAKATYDI
LTKTYTFVFT DYVNNKENIN GQFSLPLFTD RAKAPKSGTY DANINIADEM FNNKITYNYS
SPIAGIDKPN GANISSQIIG VDTASGQNTY KQTVFVNPKQ RVLGNTWVYI KGYQDKIEES
SGKVSATDTK LRIFEVNDTS KLSDSYYADP NDSNLKEVTD QFKNRIYYEH PNVASIKFGD
ITKTYVVLVE GHYDNTGKNL KTQVIQENVD PVTNRDYSIF GWNNENVVRY GGGSADGDSA
VNPKDPTPGP PVDPEPSPDP EPEPTPDPEP SPDPEPEPSP DPDPDSDSDS DSGSDSDSGS
DSDSESDSDS DSDSDSDSDS DSESDSDSES DSESDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSRVTPPN NEQKAPSNPK GEVNHSNKVS KQHKTDALPE
TGDKSENTNA TLFGAMMALL GSLLLFRKRK QDHKEKA
