| IED ID | IndEnz0002017161 |
| Enzyme Type ID | protease017161 |
| Protein Name |
ATP-dependent Clp protease proteolytic subunit 1 EC 3.4.21.92 Endopeptidase Clp 1 |
| Gene Name | clpP1 clpP Rv2461c MTV008.17c |
| 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 | MSQVTDMRSNSQGLSLTDSVYERLLSERIIFLGSEVNDEIANRLCAQILLLAAEDASKDISLYINSPGGSISAGMAIYDTMVLAPCDIATYAMGMAASMGEFLLAAGTKGKRYALPHARILMHQPLGGVTGSAADIAIQAEQFAVIKKEMFRLNAEFTGQPIERIEADSDRDRWFTAAEALEYGFVDHIITRAHVNGEAQ |
| Enzyme Length | 200 |
| Uniprot Accession Number | P9WPC5 |
| Absorption | |
| Active Site | ACT_SITE 98; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 123; /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 ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA). {ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:23314154}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (11); 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 (7) |
| Cross Reference PDB | 2C8T; 2CBY; 2CE3; 4U0G; 4U0H; 5DZK; 5E0S; 6VGK; 6VGN; 6VGQ; |
| Mapped Pubmed ID | 25267638; 26858247; 32123115; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,708 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.92; |