Detail Information for IndEnz0002005159
IED ID IndEnz0002005159
Enzyme Type ID protease005159
Protein Name Non-toxic nonhemagglutinin type A
NTNHA
Botulinum neurotoxin type A non-toxic component
Gene Name ant ntnh ACP52_06665
Organism Clostridium botulinum
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Clostridiaceae Clostridium Clostridium botulinum
Enzyme Sequence MNINDNLSINSPVDNKNVVVVRARKTDTVFKAFKVAPNIWVAPERYYGESLSIDEEYKVDGGIYDSNFLSQDSEKDKFLQAIITLLKRINSTNAGEKLLSLISTAIPFPYGYIGGGYYAPNMITFGSAPKSNKKLNSLISSTIPFPYAGYRETNYLSSEDNKSFYASNIVIFGPGANIVENNTVFYKKEDAENGMGTMTEIWFQPFLTYKYDEFYIDPAIELIKCLIKSLYFLYGIKPSDDLVIPYRLRSELENIEYSQLNIVDLLVSGGIDPKFINTDPYWFTDNYFSNAKKVFEDHRNIYETEIEGNNAIGNDIKLRLKQKFRININDIWELNLNYFSKEFSIMMPDRFNNALKHFYRKQYYKIDYPENYSINGFVNGQINAQLSLSDRNQDIINKPEEIINLLNGNNVSLMRSNIYGDGLKSTVDDFYSNYKIPYNRAYEYHFNNSNDSSLDNVNIGVIDNIPEIIDVNPYKENCDKFSPVQKITSTREINTNIPWPINYLQAQNTNNEKFSLSSDFVEVVSSKDKSLVYSFLSNVMFYLDSIKDNSPIDTDKKYYLWLREIFRNYSFDITATQEINTNCGINKVVTWFGKALNILNTSDSFVEEFQNLGAISLINKKENLSMPIIESYEIPNDMLGLPLNDLNEKLFNIYSKNTAYFKKIYYNFLDQWWTQYYSQYFDLICMAKRSVLAQETLIKRIIQKKLSYLIGNSNISSDNLALMNLTTTNTLRDISNESQIAMNNVDSFLNNAAICVFESNIYPKFISFMEQCINNINIKTKEFIQKCTNINEDEKLQLINQNVFNSLDFEFLNIQNMKSLFSSETALLIKEETWPYELVLYAFKEPGNNVIGDASGKNTSIEYSKDIGLVYGINSDALYLNGSNQSISFSNDFFENGLTNSFSIYFWLRNLGKDTIKSKLIGSKEDNCGWEIYFQDTGLVFNMIDSNGNEKNIYLSDVSNNSWHYITISVDRLKEQLLIFIDDNLVANESIKEILNIYSSNIISLLSENNPSYIEGLTILNKPTTSQEVLSNYFEVLNNSYIRDSNEERLEYNKTYQLYNYVFSDKPICEVKQNNNIYLTINNTNNLNLQASKFKLLSINPNKQYVQKLDEVIISVLDNMEKYIDISEDNRLQLIDNKNNAKKMIISNDIFISNCLTLSYNGKYICLSMKDENHNWMICNNDMSKYLYLWSFK
Enzyme Length 1193
Uniprot Accession Number Q45914
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Assembles with botulinum neurotoxin type A (BoNT/A) and protects it against pH-mediated inactivation or protease activity at pH 2.6 (the pH of the animal gastrointestinal tract) but not at pH 6.0 (PubMed:22363010). Necessary for neurotoxicity. {ECO:0000269|PubMed:22363010}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (55); Chain (1); Disulfide bond (1); Helix (35); Region (3); Site (1); Turn (6)
Keywords 3D-structure;Disulfide bond;Virulence
Interact With A5HZZ4
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: The 133-Lys-|-Lys-134 bond is cleaved during long-term storage; the cleavage site is masked in the M-PTC complex (PubMed:22363010). {ECO:0000269|PubMed:22363010}.
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 3V0A; 3V0B;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 138,093
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda