| IED ID | IndEnz0002018137 |
| Enzyme Type ID | protease018137 |
| Protein Name |
ATP-dependent Clp protease proteolytic subunit, mitochondrial EC 3.4.21.92 Endopeptidase Clp |
| Gene Name | Clpp |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MWPRVLLGEARVAVDGCRALLSRLAVHFSPPWTAVSCSPLRRSLHGTATRAFPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGSPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPELVQKETATAPTDPPAPTST |
| Enzyme Length | 272 |
| Uniprot Accession Number | O88696 |
| Absorption | |
| Active Site | ACT_SITE 149; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 174; /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:0000250|UniProtKB:Q16740}; |
| DNA Binding | |
| EC Number | 3.4.21.92 |
| Enzyme Function | FUNCTION: Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion. {ECO:0000250|UniProtKB:Q16740}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Modified residue (2); Region (1); Transit peptide (1) |
| Keywords | Acetylation;Hydrolase;Mitochondrion;Protease;Reference proteome;Serine protease;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:10754102, ECO:0000269|PubMed:22710082}. |
| Modified Residue | MOD_RES 196; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 207; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:23576753 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10347188; 10725249; 11217851; 12466851; 14610273; 14651853; 16615898; 18614015; 18799693; 19154341; 21677750; 26045162; 26058080; 26721594; 27154400; 27797820; 29420235; 29588285; 29851234; 30877431; 31939198; 32242014; 32342250; 32467259; 34943861; 9811942; |
| Motif | |
| Gene Encoded By | |
| Mass | 29,800 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.92; |