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CLFB_STAAE
ID   CLFB_STAAE              Reviewed;         913 AA.
AC   O86476; A6QKB9;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 118.
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=NWMN_2529;
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, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=9791170; DOI=10.1046/j.1365-2958.1998.01050.x;
RA   Ni Eidhin D., Perkins S., Francois P., Vaudaux P., Hoeoek M., Foster T.J.;
RT   "Clumping factor B (ClfB), a new surface-located fibrinogen-binding adhesin
RT   of Staphylococcus aureus.";
RL   Mol. Microbiol. 30:245-257(1998).
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   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   [4]
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   [5]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=12010496; DOI=10.1046/j.1365-2958.2002.02935.x;
RA   O'Brien L.M., Kerrigan S.W., Kaw G., Hogan M., Penades J., Litt D.,
RA   Fitzgerald D.J., Foster T.J., Cox D.;
RT   "Multiple mechanisms for the activation of human platelet aggregation by
RT   Staphylococcus aureus: roles for the clumping factors clfA and clfB, the
RT   serine-aspartate repeat protein sdrE and protein A.";
RL   Mol. Microbiol. 44:1033-1044(2002).
RN   [6]
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   [7]
RP   CRYSTALLIZATION.
RX   PubMed=10089377; DOI=10.1107/s0907444998012426;
RA   Deivanayagam C.C.S., Perkins S., Danthuluri S., Owens R.T., Bice T.,
RA   Nanavathy T., Foster T.J., Hoeoek M., Narayana S.V.L.;
RT   "Crystallization of ClfA and ClfB fragments: the fibrinogen-binding surface
RT   proteins of Staphylococcus aureus.";
RL   Acta Crystallogr. D 55:554-556(1999).
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:12010496,
CC       ECO:0000269|PubMed:12427098, ECO:0000269|PubMed:15385531,
CC       ECO:0000269|PubMed:9791170}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305|PubMed:9791170};
CC       Peptidoglycan-anchor {ECO:0000305|PubMed:9791170}. Note=Anchored to the
CC       cell wall by sortase A (By similarity). {ECO:0000250|UniProtKB:Q2FUY2}.
CC   -!- INDUCTION: Expressed on cells only at early exponential phase with
CC       aeration. {ECO:0000269|PubMed:12010496, ECO:0000269|PubMed:9791170}.
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   -!- MISCELLANEOUS: Fg-binding activity of ClfB is regulated by the divalent
CC       cations Ca(2+) and Mn(2+).
CC   -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC       (SDr) family. {ECO:0000305}.
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DR   EMBL; AJ224764; CAA12115.1; -; Genomic_DNA.
DR   EMBL; AP009351; BAF68801.1; -; Genomic_DNA.
DR   RefSeq; WP_000745871.1; NZ_CP023390.1.
DR   AlphaFoldDB; O86476; -.
DR   SMR; O86476; -.
DR   EnsemblBacteria; BAF68801; BAF68801; NWMN_2529.
DR   KEGG; sae:NWMN_2529; -.
DR   HOGENOM; CLU_004137_2_0_9; -.
DR   OMA; KPVHPSI; -.
DR   PRO; PR:O86476; -.
DR   Proteomes; UP000006386; 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; Secreted; Signal; Virulence.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..877
FT                   /note="Clumping factor B"
FT                   /id="PRO_0000042004"
FT   PROPEP          878..913
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000042005"
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..885
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           874..878
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..834
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..861
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..877
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         877
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   CONFLICT        142
FT                   /note="A -> G (in Ref. 1; CAA12115)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   913 AA;  97262 MW;  AAE5B51271B78941 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 DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSESDSDS ESDSESDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     RVTPPNNEQK APSNPKGEVN HSNKVSKQHK TDALPETGDK SENTNATLFG AMMALLGSLL
     LFRKRKQDHK EKA
 
 
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