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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
 
 
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