ID A0A1B4Z3Z2_CLOBO Unreviewed; 372 AA. AC A0A1B4Z3Z2; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 11-DEC-2019, entry version 13. 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: Sulfhydryl-activated toxin that causes cytolysis by forming CC pores in cholesterol containing host membranes. After binding to target CC membranes, the protein undergoes a major conformation change, leading CC to its insertion in the host membrane and formation of an oligomeric CC pore complex. {ECO:0000256|RuleBase:RU364025}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU364025}. Host CC cell membrane {ECO:0000256|RuleBase:RU364025}; Multi-pass membrane CC 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: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:InterPro. 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|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 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 //