ID A0A1B4Z3Z2_CLOBO Unreviewed; 372 AA. AC A0A1B4Z3Z2; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 07-OCT-2020, entry version 15. DE RecName: Full=Thiol-activated cytolysin {ECO:0000256|RuleBase:RU364025}; DE Flags: Fragment; GN Name=bly1 {ECO:0000313|EMBL:BAV54145.1}; OS Clostridium botulinum D. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=36829 {ECO:0000313|EMBL:BAV54145.1}; RN [1] {ECO:0000313|EMBL:BAV54145.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4947 {ECO:0000313|EMBL:BAV54145.1}; RX PubMed=27825483; DOI=10.1016/j.micres.2016.08.011; RA Suzuki T., Nagano T., Niwa K., Mutoh S., Uchino M., Tomizawa M., Sagane Y., RA Watanabe T.; RT "Isolation of botulinolysin, a thiol-activated hemolysin, from serotype D RT Clostridium botulinum: A species-specific gene duplication in Clostridia."; RL Microbiol. Res. 193:20-29(2016). CC -!- FUNCTION: A cholesterol-dependent toxin that causes cytolysis by CC forming pores in cholesterol containing host membranes. After binding CC to target membranes, the protein undergoes a major conformation change, CC leading to its insertion in the host membrane and formation of an CC oligomeric pore complex. Cholesterol is required for binding to host CC membranes, membrane insertion and pore formation; cholesterol binding CC is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly CC inactivated by oxidation. {ECO:0000256|RuleBase:RU364025}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Secreted CC {ECO:0000256|RuleBase:RU364025}. Host cell membrane CC {ECO:0000256|RuleBase:RU364025}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU364025}. CC -!- SIMILARITY: Belongs to the cholesterol-dependent cytolysin family. CC {ECO:0000256|ARBA:ARBA00008503, ECO:0000256|RuleBase:RU364025}. 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; LC149614; BAV54145.1; -; Genomic_DNA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015485; F:cholesterol binding; IEA:InterPro. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.1430; -; 1. DR Gene3D; 3.90.840.10; -; 1. DR InterPro; IPR035390; Thiol_cytolys_C. DR InterPro; IPR038700; Thiol_cytolys_C_sf. DR InterPro; IPR001869; Thiol_cytolysin. DR InterPro; IPR036363; Thiol_cytolysin_ab_sf. DR InterPro; IPR036359; Thiol_cytolysin_sf. DR Pfam; PF17440; Thiol_cytolys_C; 1. DR Pfam; PF01289; Thiol_cytolysin; 1. DR PRINTS; PR01400; TACYTOLYSIN. DR SUPFAM; SSF56978; SSF56978; 1. PE 3: Inferred from homology; KW Cytolysis {ECO:0000256|ARBA:ARBA00022852, ECO:0000256|RuleBase:RU364025}; KW Hemolysis {ECO:0000256|ARBA:ARBA00022735, ECO:0000256|RuleBase:RU364025}; KW Host cell membrane {ECO:0000256|RuleBase:RU364025}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, KW ECO:0000256|RuleBase:RU364025}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121, KW ECO:0000256|RuleBase:RU364025}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364025}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364025}; KW Toxin {ECO:0000256|ARBA:ARBA00022656, ECO:0000256|RuleBase:RU364025}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU364025}; KW Transmembrane beta strand {ECO:0000256|ARBA:ARBA00022452, KW ECO:0000256|RuleBase:RU364025}; Virulence {ECO:0000256|ARBA:ARBA00023026}. FT DOMAIN 302..368 FT /note="Thiol_cytolys_C" FT /evidence="ECO:0000259|Pfam:PF17440" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAV54145.1" FT NON_TER 372 FT /evidence="ECO:0000313|EMBL:BAV54145.1" SQ SEQUENCE 372 AA; 41374 MW; F95D40393F95801F CRC64; SQSIDSINDR TYPGAIQLAN RNLIENKPDL VSCERKPITI SVDLPGMTSD GKKVVKSPTY SSVNSAINSI LDTWNTKYSQ KYTIPTRVSY SDTMVYSKSQ LSTMLGCNFK SIDKSLNIDF NSIFKGEKKV MVVAYKQIFY TVSVDAPNRP SDVFEDNVTF NELALKGLNN NNPPAYVSNV AYGRTIYVKL ETTSKSGNVK AAFKALIDNQ DISSNAEYKD ILNQSSFTAT VLGGGAQEHN KIVTKDFDEI RNVIKNNSVY SPQNPGYPIS YTTTFLKDNH IASINNKTEY VETTATEYNN GKIVLDHSGA YVAQFQVTWD EVSYDKQGNE IVEHKGWSGN NTDKTAHFNT EIYLKGNARN ISVQIKDARL AG //