| IED ID | IndEnz0002015872 |
| Enzyme Type ID | protease015872 |
| Protein Name |
ATP-dependent Clp protease proteolytic subunit EC 3.4.21.92 Endopeptidase Clp |
| Gene Name | clpP Ecaj_0202 |
| Organism | Ehrlichia canis (strain Jake) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rickettsiales Anaplasmataceae Ehrlichia canis group Ehrlichia canis Ehrlichia canis (strain Jake) |
| Enzyme Sequence | MTLVPMVVEQTSRGERAYDIYSRLLKERIIFITGPIEDQMASLVVAQLVFLEAENPEKEICMYINSPGGVVTAGLSIYDTMQYIKPKVSTLCLGQAASMGSLLLAAGEPGMRYALPNSRIMIHQPSGGFQGQATDIEIHAKEILDIKSRLNDIYVKHTGRDLPEVVANMERDNFMRAEKAKDFGIIDKVIEKRLDIEESN |
| Enzyme Length | 200 |
| Uniprot Accession Number | Q3YSQ3 |
| 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 | 22,307 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |