| IED ID | IndEnz0002004522 |
| Enzyme Type ID | protease004522 |
| Protein Name |
ATP-dependent Clp protease proteolytic subunit EC 3.4.21.92 Endopeptidase Clp |
| Gene Name | clpP |
| Organism | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Chlorophyta core chlorophytes Chlorophyceae CS clade Chlamydomonadales Chlamydomonadaceae Chlamydomonas Chlamydomonas reinhardtii (Chlamydomonas smithii) |
| Enzyme Sequence | MPIGVPRIIYCWGEELPAQWTDIYNFIFRRRMVFLMQYLDDELCNQICGLLINIHMEDRSKELEKKEMEKSGLFKSGTAKTKGKDTVKKENLSGGASAKRQSVEDLLTSDNDFGIEENHLLEQYTLQKITTEWLNWNAQFFDYSDEPYLYYLADILSKDFSPNQDKDSANLNFAKSSANKQAFQNPAEMTKLIKNLKNLKNFSTGSKNVKQNLDVYSPFRLLANFAPQNYNLEHPNQNLAEIYSLLKTSTQNTNQPFTKKLIDNLSHKELMNRLQSPEKLVASSEKALGRRRLKQRYVQERLGSGGLSNSKALKAYNYLDQGALNNESGRSLYRKQTERVIQEEESKKVFMIINSFGGSVGNGITVHDALQFIKAGSLTLALGVAASAASLALAGGTIGERYVTEGCHTMIHQPEGGLNGQASDIWIDSQEIMKIRLDVAEIYSLSTYRPRHKILRDLDRDFYLTAMETIYYGLADEIATNEVMHSIVEMTNQVWSYHDSKQERLLESRASLVGDSTQTQESNS |
| Enzyme Length | 524 |
| Uniprot Accession Number | P42380 |
| Absorption | |
| Active Site | ACT_SITE 387; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10085, ECO:0000255|PROSITE-ProRule:PRU10086"; ACT_SITE 412; /evidence="ECO:0000250" |
| 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|PROSITE-ProRule:PRU10085, ECO:0000255|PROSITE-ProRule:PRU10086}; |
| 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). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Natural variant (1); Region (2) |
| Keywords | 3D-structure;Chloroplast;Hydrolase;Plastid;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (2) |
| Cross Reference PDB | 7EKO; 7EKQ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | Chloroplast |
| Mass | 59,501 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.92; |