ID Q57236_CLOBO Unreviewed; 1278 AA. AC Q57236; Q45863; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 29-SEP-2021, entry version 136. DE SubName: Full=Botulinum neurotoxin type F {ECO:0000313|EMBL:ADA79552.1}; DE SubName: Full=Neurotoxin type F {ECO:0000313|EMBL:AAA23210.1}; GN Name=F {ECO:0000313|EMBL:AAA23210.1}; GN Synonyms=bonT {ECO:0000313|EMBL:AAA23210.1}; OS Clostridium botulinum. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1491 {ECO:0000313|EMBL:AAA23210.1}; RN [1] {ECO:0000313|EMBL:AAA23210.1} RP NUCLEOTIDE SEQUENCE. RA Elmore M.J., Bodsworth N.J., Whelan S.M., Minton N.P.; RT "The complete nucleotide sequence of the gene coding for proteolytic type F RT neurotoxin of Clostridium botulinum."; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADA79552.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=12F {ECO:0000313|EMBL:ADA79552.1}, 4VI RC {ECO:0000313|EMBL:ADA79553.1}, 4VII {ECO:0000313|EMBL:ADA79554.1}, 8g RC {ECO:0000313|EMBL:ADA79555.1}, and Pasteurized Crab RC {ECO:0000313|EMBL:ADA79556.1}; RX PubMed=20511432; DOI=10.1128/AEM.03109-09; RA Raphael B.H., Choudoir M.J., Luquez C., Fernandez R., Maslanka S.E.; RT "Sequence diversity of genes encoding botulinum neurotoxin type F."; RL Appl. Environ. Microbiol. 76:4805-4812(2010). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- INTERACTION: CC Q57236; P63027: VAMP2; Xeno; NbExp=3; IntAct=EBI-15790260, EBI-520113; CC -!- SIMILARITY: Belongs to the peptidase M27 family. CC {ECO:0000256|ARBA:ARBA00007113}. 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; L35496; AAA23210.1; -; Genomic_DNA. DR EMBL; GU213204; ADA79552.1; -; Genomic_DNA. DR EMBL; GU213205; ADA79553.1; -; Genomic_DNA. DR EMBL; GU213206; ADA79554.1; -; Genomic_DNA. DR EMBL; GU213207; ADA79555.1; -; Genomic_DNA. DR EMBL; GU213208; ADA79556.1; -; Genomic_DNA. DR PIR; S48110; S48110. DR RefSeq; WP_011987710.1; NZ_LFPF01000007.1. DR DIP; DIP-48535N; -. DR IntAct; Q57236; 1. DR PATRIC; fig|1491.420.peg.3551; -. DR BRENDA; 3.4.24.69; 1462. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IEA:InterPro. DR Gene3D; 1.20.1120.10; -; 1. DR InterPro; IPR000395; Bot/tetX_LC. DR InterPro; IPR036248; Clostridium_toxin_transloc. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf. DR InterPro; IPR013104; Toxin_rcpt-bd_C. DR InterPro; IPR012928; Toxin_rcpt-bd_N. DR InterPro; IPR012500; Toxin_trans. DR Pfam; PF01742; Peptidase_M27; 1. DR Pfam; PF07951; Toxin_R_bind_C; 1. DR Pfam; PF07953; Toxin_R_bind_N; 1. DR Pfam; PF07952; Toxin_trans; 1. DR PRINTS; PR00760; BONTOXILYSIN. DR SUPFAM; SSF49899; SSF49899; 1. DR SUPFAM; SSF50386; SSF50386; 1. DR SUPFAM; SSF58091; SSF58091; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Neurotoxin {ECO:0000256|ARBA:ARBA00022699, ECO:0000313|EMBL:AAA23210.1}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Toxin {ECO:0000256|ARBA:ARBA00022656}; KW Virulence {ECO:0000256|ARBA:ARBA00023026}. FT DOMAIN 4..409 FT /note="Peptidase_M27" FT /evidence="ECO:0000259|Pfam:PF01742" FT DOMAIN 538..848 FT /note="Toxin_trans" FT /evidence="ECO:0000259|Pfam:PF07952" FT DOMAIN 878..1072 FT /note="Toxin_R_bind_N" FT /evidence="ECO:0000259|Pfam:PF07953" FT DOMAIN 1085..1277 FT /note="Toxin_R_bind_C" FT /evidence="ECO:0000259|Pfam:PF07951" FT COILED 717..737 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 763..783 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 1278 AA; 147075 MW; A1BE1318431D6918 CRC64; MPVVINSFNY NDPVNDDTIL YMQIPYEEKS KKYYKAFEIM RNVWIIPERN TIGTDPSDFD PPASLENGSS AYYDPNYLTT DAEKDRYLKT TIKLFKRINS NPAGEVLLQE ISYAKPYLGN EHTPINEFHP VTRTTSVNIK SSTNVKSSII LNLLVLGAGP DIFENSSYPV RKLMDSGGVY DPSNDGFGSI NIVTFSPEYE YTFNDISGGY NSSTESFIAD PAISLAHELI HALHGLYGAR GVTYKETIKV KQAPLMIAEK PIRLEEFLTF GGQDLNIITS AMKEKIYNNL LANYEKIATR LSRVNSAPPE YDINEYKDYF QWKYGLDKNA DGSYTVNENK FNEIYKKLYS FTEIDLANKF KVKCRNTYFI KYGFLKVPNL LDDDIYTVSE GFNIGNLAVN NRGQNIKLNP KIIDSIPDKG LVEKIVKFCK SVIPRKGTKA PPRLCIRVNN RELFFVASES SYNENDINTP KEIDDTTNLN NNYRNNLDEV ILDYNSETIP QISNQTLNTL VQDDSYVPRY DSNGTSEIEE HNVVDLNVFF YLHAQKVPEG ETNISLTSSI DTALSEESQV YTFFSSEFIN TINKPVHAAL FISWINQVIR DFTTEATQKS TFDKIADISL VVPYVGLALN IGNEVQKENF KEAFELLGAG ILLEFVPELL IPTILVFTIK SFIGSSENKN KIIKAINNSL MERETKWKEI YSWIVSNWLT RINTQFNKRK EQMYQALQNQ VDAIKTVIEY KYNNYTSDER NRLESEYNIN NIREELNKKV SLAMENIERF ITESSIFYLM KLINEAKVSK LREYDEGVKE YLLDYISEHR SILGNSVQEL NDLVTSTLNN SIPFELSSYT NDKILILYFN KLYKKIKDNS ILDMRYENNK FIDISGYGSN ISINGDVYIY STNRNQFGIY SSKPSEVNIA QNNDIIYNGR YQNFSISFWV RIPKYFNKVN LNNEYTIIDC IRNNNSGWKI SLNYNKIIWT LQDTAGNNQK LVFNYTQMIS ISDYINKWIF VTITNNRLGN SRIYINGNLI DEKSISNLGD IHVSDNILFK IVGCNDTRYV GIRYFKVFDT ELGKTEIETL YSDEPDPSIL KDFWGNYLLY NKRYYLLNLL RTDKSITQNS NFLNINQQRG VYQKPNIFSN TRLYTGVEVI IRKNGSTDIS NTDNFVRKND LAYINVVDRD VEYRLYADIS IAKPEKIIKL IRTSNSNNSL GQIIVMDSIG NNCTMNFQNN NGGNIGLLGF HSNNLVASSW YYNNIRKNTS SNGCFWSFIS KEHGWQEN //