| IED ID | IndEnz0002005586 |
| Enzyme Type ID | protease005586 |
| Protein Name |
Botulinum-like toxin eBoNT/J eBoNT/J Cleaved into: Botulinum-like toxin eBoNT/J light chain LC EC 3.4.24.69 ; Botulinum-like toxin eBoNT/J heavy chain HC |
| Gene Name | A5816_002916 |
| Organism | Enterococcus sp. (strain 3G1_DIV0629) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Enterococcaceae Enterococcus unclassified Enterococcus Enterococcus sp. (strain 3G1_DIV0629) |
| Enzyme Sequence | MVTINDLHYSDPIDEDNIINMRIPLYDLEVDDQFINHNVPDLKAFQVFPNVWVVPERYTFYSTMKNLDAPANPSRSSYYDPTYLQSDAEKEVFLQQMILLFKRINSTQEGQQFLNLLSRSIPVPYESNGDVAMGTTQVIKQMDDKGNVLKHRRAHIIIYGPGPDLMAKGSKALTKSRETGRGCMAEIYFSPMYHKTYSTKLTNKNSLVDKSVQEFVPDPAVTLIHELCHGLHALYGIDLGNVGSWEFNSNPNSLFSSWFSSKEAVNFEEVMTFGGEDVKVIKSEIDKKIPGILNLIKTTVEPIINKITDPHDEMLQCLQSKYPSLKGTLGQFFFDDTQLEKDIRDLWMVMNETMFAENLKALTRARYLVPKVENIVQVDILSPNVYTIDKGFNHLSKGFKGQSVSQSYFRKISALARGAVVRACPNPHFSSQRGLSSCIEILEDDLFIMSSKDSFTDTDFSEPSVGPVSYKAKKGADTILDSTLSNYDFSKEINFTSTVPIITVEDPLETDEDVPVISEDRTVYVDDYTTFHFLEAQKIGKEVVPTQTKVVFTTNMEEALFDSKKVYTVFENTASRINEAGTGIANGMMFYQWLKGIVQDFTEEATQKDTFDKISDVTMIVPYLGNILNIGNDIRKGDFMGAVELGGVTILLEAIPELTLPVLIGLTIIEDELEKEQVSQTVYNVLDKRDEKWEEVYGFVKQQWWWMVHTQFETRILHAYQALNHQVEAIKANMTYQLANYRGNQEDKELLEKAIDDTLQSLYYAVDQAMHNIKRFLIQSSKSYLLNQMLPKTKEQLLAFDQQTLRNVNDFINKNQGVLGESLAKDLKKKVEKRLTSLPVFNLEDLPISEFEDLIHSHEIDIQDSEVLNIGVNNGKIQDLSGENTPLTLGENLHIVNGRDNQAVRLNNQLDSKLEIQSRPNIHFTAFEDFSISIWIRCSMLRNNRNRGQKYTIIQQFNKYGWQLAIQDSVFVWTLHDTFNNQIQLTSGSALTNKNYLLQNFWLHITVTNKRSEKSRLYINGVLQDQKDISVLGNCHPKEPILFSIQDNSDPNYFVRFEQFNVYRKALTDSEVNRLYWKYFEGSYLRDVWGERLTYNRDYYMQLSTLPGRGIKREYRTWSGFDYIILSELGTQKIPTHEVTYPKLYQGQKITIHSDGKNLEPHVKSNKNIRLKIDDFYIGVVNPFKLPEWRPESGAYVVTTYNHAEDLCLYFRTRSSSQSLYYGQLIMNDGRNKSLLNYTLKGSTYWIWSSAWYYENYNTSSKTAGNWYFIPVDEGWKED |
| Enzyme Length | 1279 |
| Uniprot Accession Number | A0A242DI27 |
| Absorption | |
| Active Site | ACT_SITE 226; /evidence="ECO:0000250|UniProtKB:P0DPI0, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.; EC=3.4.24.69; Evidence={ECO:0000250|UniProtKB:P0DPI0}; |
| DNA Binding | |
| EC Number | 3.4.24.69 |
| Enzyme Function | FUNCTION: Strongly resembles a botulinum-type toxin, with the appropriate domains and residues to have proteolytic function, although its C-terminus (which binds to a eukaryotic host cell) is different enough from clostrial botulinum toxins that it might bind another cell target (PubMed:29323697). Might be a precursor of a toxin that binds to an unknown eukaryotic cell receptor(s), and be taken up into the host cell via the endocytic pathway. When the pH of the putative toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the heavy chain forms pores that allows the light chain to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and light chain cleaves its target protein (By similarity). {ECO:0000250|UniProtKB:P0DPI0, ECO:0000305|PubMed:29323697}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (3); Disulfide bond (1); Metal binding (3); Motif (1); Region (4) |
| Keywords | Disulfide bond;Host cell membrane;Host cytoplasm;Host cytoplasmic vesicle;Host membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Neurotoxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Botulinum-like toxin eBoNT/J]: Secreted {ECO:0000250|UniProtKB:P0DPI0}.; SUBCELLULAR LOCATION: [Botulinum-like toxin eBoNT/J light chain]: Secreted {ECO:0000250|UniProtKB:P0DPI0}. Host cytoplasm, host cytosol {ECO:0000250|UniProtKB:P0DPI0}.; SUBCELLULAR LOCATION: [Botulinum-like toxin eBoNT/J heavy chain]: Secreted {ECO:0000250|UniProtKB:P0DPI0}. Host cell membrane {ECO:0000250|UniProtKB:P0DPI0}. Host cytoplasmic vesicle membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0DPI0}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 1250..1253; /note="Host ganglioside-binding motif"; /evidence="ECO:0000250|UniProtKB:P0DPI0, ECO:0000305|PubMed:29323697" |
| Gene Encoded By | |
| Mass | 147,267 |
| Kinetics | |
| Metal Binding | METAL 225; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000250|UniProtKB:P0DPI0, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:29323697"; METAL 229; /note="Zinc; via tele nitrogen; catalytic"; /evidence="ECO:0000250|UniProtKB:P0DPI0, ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:29323697"; METAL 269; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P0DPI0, ECO:0000305|PubMed:29323697" |
| Rhea ID | |
| Cross Reference Brenda |