CLFB_STAAW
ID CLFB_STAAW Reviewed; 907 AA.
AC Q8NUL0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=MW2551;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}. Note=Anchored to the cell wall by sortase A (By
CC similarity). {ECO:0000250|UniProtKB:Q2FUY2}.
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. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by aureolysin (aur). This cleavage leads
CC to the inactivation of ClfB (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; BA000033; BAB96416.1; -; Genomic_DNA.
DR RefSeq; WP_000745817.1; NC_003923.1.
DR AlphaFoldDB; Q8NUL0; -.
DR SMR; Q8NUL0; -.
DR PRIDE; Q8NUL0; -.
DR EnsemblBacteria; BAB96416; BAB96416; BAB96416.
DR KEGG; sam:MW2551; -.
DR HOGENOM; CLU_004137_2_0_9; -.
DR OMA; KPVHPSI; -.
DR PRO; PR:Q8NUL0; -.
DR Proteomes; UP000000418; 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 3: Inferred from homology;
KW Cell wall; Peptidoglycan-anchor; Secreted; Signal; Virulence.
FT SIGNAL 1..44
FT /evidence="ECO:0000250"
FT CHAIN 45..871
FT /note="Clumping factor B"
FT /id="PRO_0000042016"
FT PROPEP 872..907
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000042017"
FT REGION 44..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..542
FT /note="Ligand binding A region"
FT /evidence="ECO:0000250"
FT REGION 530..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..26
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000250|UniProtKB:Q2FUY2"
FT MOTIF 272..276
FT /note="MIDAS-like motif"
FT MOTIF 868..872
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..828
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 197..198
FT /note="Cleavage; by aureolysin"
FT /evidence="ECO:0000250"
FT SITE 199..200
FT /note="Cleavage; by aureolysin"
FT /evidence="ECO:0000250"
FT MOD_RES 871
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 907 AA; 96614 MW; BD951754BC1FE638 CRC64;
MKKRIDYLSN KQNKYSIRRF TVGTTSVIVG ATILFGIGNH QAQASEQSND TTQSSKNNAS
ADSEKNNMIE TPQLNTTAND TSDISANTNS ANVDSTAKPM STQTSNTTTT EPASTNETPQ
LTAIKDQATA AKMQDQTVPQ EANSQVDNKT TNDANSIATN SELKNPQTLD LPQSSPQTIS
NAQGTSKPSV RTRAVRSLAV AEPVVNAADA KGTNVNDKVT AKDFQLEKTT FDPNQSGNTF
MAANFTVTGQ VKSGDYFTAK LPDSVTGNGD VDYSNSNNTM PIADIVNDKN EVVAKATYDI
LTKTYTFVFT DYVNDKQNIN GKFSLPLFTD RAKAPKSGTY DANINIADEM FNNKITYNYS
SPIAGIDKPN GANISSQIIG VDTASGQNTY KQTVFVNPKQ RVLGNTWVYI KGYQDKIEES
SGKVSATDTK LRIFEVNDTS KLSDSYYADP NDSNLKEVTD QFKDKITYKY QNVASINFGD
INKTYVVLVE GHYDKTGKNL KTQVIQENVD PATGKDYSIF GWNNENVVRY GGGSADGDSA
VNPKDPTPGP PVDPEPSPDP EPEPSPDPDP EPTPDPEPSP DPDPDSDSDS DSGSDSDSDS
DSDSDSDSDS GSDSDSDSDS DSESDSESDS DSDSESDSDS DSDSESDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSESDSDSDS DSESDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSES DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSESDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSESDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSRVTPPN
NEQKAPSNPK GEVNHSNKVS KQHKTDALPE TGDKSENTNA TLFGAMMALL GSLLLFRKRK
QDHKEKA
