IED ID | IndEnz0002017937 |
Enzyme Type ID | protease017937 |
Protein Name |
ATP-dependent Clp protease proteolytic subunit EC 3.4.21.92 Endopeptidase Clp |
Gene Name | clpP Hore_14940 |
Organism | Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Halanaerobiales Halanaerobiaceae Halothermothrix Halothermothrix orenii Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562) |
Enzyme Sequence | MSLIPVVVEQTNRGERSYDIYSRLLKDRIVFLGHPINDELSNLIIAQLLFLEAEDPDKDIHLYINSPGGSVTAALAMYDTIQYIKPDVATICMGQAASAGALLLASGTKGKRYALPNARVMIHQPAGGVQGKATEAEIHIKELLRLRERLNEILSKHTGKSVEQISKDVEQDYFMTAEEALEYGIIDEVITKNELKDK |
Enzyme Length | 198 |
Uniprot Accession Number | B8CY74 |
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. {ECO:0000255|HAMAP-Rule:MF_00444}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1) |
Keywords | 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 | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 21,980 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |