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 27-MAR-2024, entry version 110. 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; Bacillota; 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}. 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; 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 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 Gene3D; 2.60.40.1290; -; 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 NCBIfam; TIGR01167; LPXTG_anchor; 1. DR NCBIfam; NF033845; MSCRAMM_ClfB; 1. DR NCBIfam; TIGR01168; YSIRK_signal; 1. DR PANTHER; PTHR34403:SF8; RETINITIS PIGMENTOSA 1-LIKE 1 PROTEIN-LIKE; 1. DR PANTHER; PTHR34403; TOL-PAL SYSTEM PROTEIN TOLA; 1. 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; Bacterial adhesins; 2. 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 //