ID HLYB_BRAHO Reviewed; 828 AA.
AC Q54316;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Hemolysin B;
GN Name=tlyB;
OS Brachyspira hyodysenteriae (Treponema hyodysenteriae).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=159;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B204;
RX PubMed=7968456; DOI=10.1006/mpat.1994.1028;
RA Ter Huurne A.A.H.M., Muir S., van Houten M., van der Zeijst B.A.M.,
RA Gaastra W., Kusters J.G.;
RT "Characterization of three putative Serpulina hyodysenteriae hemolysins.";
RL Microb. Pathog. 16:269-282(1994).
CC -!- FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell
CC membranes and cause cell rupture by mechanisms not clearly defined.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC {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; X73140; CAA51655.1; -; Genomic_DNA.
DR AlphaFoldDB; Q54316; -.
DR SMR; Q54316; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytolysis; Hemolysis; Nucleotide-binding; Repeat;
KW Toxin; Virulence.
FT CHAIN 1..828
FT /note="Hemolysin B"
FT /id="PRO_0000191229"
FT DOMAIN 4..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT DOMAIN 426..461
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT REGION 7..72
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 83..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 172..419
FT /note="I"
FT REGION 480..671
FT /note="II"
FT BINDING 217..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 554..561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 828 AA; 93311 MW; 2F7E1183000438C2 CRC64;
MFQFHLTSKA KKVIELYAQE EAKRLNHDMV TPEHILLGLL YESEALATRV LMRLKIDLDR
LKLELESAMV KSSTTKVFGT LPTAPRVQKL ISRSAEEARA LSHNYIGTEH LLLGLLREES
GTAYNVLTSM GLELTILRQE ILKMLGVAGS NISSMEQTSQ EDNVKKVKTP TLDQFARDLT
KMARDKALDR VIGRENEVMR VVQILSRRKK NNPILLGEPG VGKTAIVEGL AEKIVAADVP
DILLKKRVLT LDLSSVVAGT KYRGEFEERI KNIVLEIKKA SNIIIFIDEL HTLIGAGGAE
GALDAANMLK PALSRGEIQC IGATTINEYK KYIEKDGALV RRFQPINVEE PSIEDTIEIL
NGIKGKYEEH HKVKYTDEAI NAAAVLSKRY IFERHLPDKA IDLIDEAGSR ARLLNMTRPQ
EFKDLEKKIE ELNQQKKRVV ESQNFEDAAK IRDEITSLQE ELSKKEEKCR EEREKIETFI
EEDDIRHVIS EITNIPIKRL LNSESKRLIG MEEELHQKVV GQKEAISSIS KAIRRSRAGL
KTSKRPLGSF IFLGPTGVGK TALAKVLSEF MFGDSDALIR IDMSEFMEKF AVSRLIGAPP
GYVGYEEGGG LTEKVRRKPY SLILFDEIEK AHPDVTNILL QVLEEGQLTD NFGRKVDFSN
TIIIITSNLG ARDIVKGSSL GFNAVGSEKD ANDIKNFALE ELKQNFNPEF LNRIDDIIVF
HTLSKEDLKD IINIMLKELN EAIKERNIVI NLSEEAKNYI IDKGFDKKYG ARSLRRAIQK
EIEDYVSTEI LFGNIEDGDT INVDRNDGSL IFSYDKSVKT ENKELSKS
//
