CLFB_STAAN
ID CLFB_STAAN Reviewed; 877 AA.
AC Q7A382;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=SA2423;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000018; BAB43728.1; -; Genomic_DNA.
DR PIR; F90070; F90070.
DR RefSeq; WP_000745891.1; NC_002745.2.
DR PDB; 3ASW; X-ray; 2.60 A; A=212-531.
DR PDB; 3AT0; X-ray; 2.50 A; A=212-541.
DR PDB; 3AU0; X-ray; 2.45 A; A=203-541.
DR PDBsum; 3ASW; -.
DR PDBsum; 3AT0; -.
DR PDBsum; 3AU0; -.
DR AlphaFoldDB; Q7A382; -.
DR SMR; Q7A382; -.
DR EnsemblBacteria; BAB43728; BAB43728; BAB43728.
DR KEGG; sau:SA2423; -.
DR HOGENOM; CLU_004137_2_0_9; -.
DR OMA; KPVHPSI; -.
DR EvolutionaryTrace; Q7A382; -.
DR PRO; PR:Q7A382; -.
DR Proteomes; UP000000751; 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 3D-structure; Cell wall; Peptidoglycan-anchor; Secreted; Signal; Virulence.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..841
FT /note="Clumping factor B"
FT /id="PRO_0000042010"
FT PROPEP 842..877
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000042011"
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 /evidence="ECO:0000250"
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:0000250|UniProtKB:Q2FUY2"
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 /evidence="ECO:0000250"
FT SITE 199..200
FT /note="Cleavage; by aureolysin"
FT /evidence="ECO:0000250"
FT MOD_RES 841
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3AU0"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:3AU0"
FT TURN 274..278
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:3AU0"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:3AU0"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 320..329
FT /evidence="ECO:0007829|PDB:3AU0"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 374..381
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 403..415
FT /evidence="ECO:0007829|PDB:3AU0"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:3AU0"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:3AU0"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:3AU0"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 473..481
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 485..493
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 500..509
FT /evidence="ECO:0007829|PDB:3AU0"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:3AU0"
FT STRAND 518..526
FT /evidence="ECO:0007829|PDB:3AU0"
SQ SEQUENCE 877 AA; 93651 MW; F0EF0A57AFDB357F 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 DSDSDSESDS DSDSDSDSDS
DSDSESDSDS ESDSESDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSESDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSRVTPPN NEQKAPSNPK GEVNHSNKVS KQHKTDALPE
TGDKSENTNA TLFGAMMALL GSLLLFRKRK QDHKEKA
