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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
