IED ID | IndEnz0002017418 |
Enzyme Type ID | protease017418 |
Protein Name |
ATP-dependent Clp protease proteolytic subunit 2 EC 3.4.21.92 Endopeptidase Clp 2 |
Gene Name | clpP2 Rv2460c MTV008.16c |
Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Enzyme Sequence | MNSQNSQIQPQARYILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLESLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAVLLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTLMETTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLSAQTA |
Enzyme Length | 214 |
Uniprot Accession Number | P9WPC3 |
Absorption | |
Active Site | ACT_SITE 110; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 135; /evidence=ECO:0000255|HAMAP-Rule:MF_00444 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).; EC=3.4.21.92; Evidence={ECO:0000255|HAMAP-Rule:MF_00444}; |
DNA Binding | |
EC Number | 3.4.21.92 |
Enzyme Function | FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1. Does not seem to act on anti-sigma-L factor RslA. {ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:20025669, ECO:0000269|PubMed:23314154}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (12); Chain (1); Helix (7); Turn (1) |
Keywords | 3D-structure;Cytoplasm;Hydrolase;Protease;Reference proteome;Serine protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | Electron microscopy (3); X-ray crystallography (3) |
Cross Reference PDB | 4U0G; 5DZK; 5E0S; 6VGK; 6VGN; 6VGQ; |
Mapped Pubmed ID | 16844784; 25267638; 26858247; 32123115; |
Motif | |
Gene Encoded By | |
Mass | 23,540 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.21.92; |