ID A0A1B4Z3Z2_CLOBO Unreviewed; 372 AA. AC A0A1B4Z3Z2; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 30-AUG-2017, entry version 7. 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., RA Sagane Y., Watanabe T.; RT "Isolation of botulinolysin, a thiol-activated hemolysin, from RT serotype D Clostridium botulinum: A species-specific gene duplication RT in Clostridia."; RL Microbiol. Res. 193:20-29(2016). CC -!- FUNCTION: Sulfhydryl-activated toxin that causes cytolysis by CC forming pores in cholesterol containing host membranes. After CC binding to target membranes, the protein undergoes a major CC conformation change, leading to its insertion in the host membrane CC and formation of an oligomeric pore complex. CC {ECO:0000256|RuleBase:RU364025}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU364025}. CC Host cell membrane {ECO:0000256|RuleBase:RU364025}; Multi-pass CC membrane protein {ECO:0000256|RuleBase:RU364025}. CC -!- SIMILARITY: Belongs to the thiol-activated cytolysin family. CC {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:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:InterPro. DR Gene3D; 3.90.840.10; -; 2. DR InterPro; IPR035390; Thiol_cytolys_C. DR InterPro; IPR001869; Thiol_cytolysin. 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|RuleBase:RU364025}; KW Hemolysis {ECO:0000256|RuleBase:RU364025}; KW Host cell membrane {ECO:0000256|RuleBase:RU364025}; KW Host membrane {ECO:0000256|RuleBase:RU364025}; KW Lipid-binding {ECO:0000256|RuleBase:RU364025}; KW Membrane {ECO:0000256|RuleBase:RU364025}; KW Secreted {ECO:0000256|RuleBase:RU364025}; KW Toxin {ECO:0000256|RuleBase:RU364025}; KW Transmembrane {ECO:0000256|RuleBase:RU364025}; KW Transmembrane beta strand {ECO:0000256|RuleBase:RU364025}. FT DOMAIN 302 368 Thiol_cytolys_C. {ECO:0000259|Pfam: FT PF17440}. FT NON_TER 1 1 {ECO:0000313|EMBL:BAV54145.1}. FT NON_TER 372 372 {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 //