| IED ID | IndEnz0002017976 |
| Enzyme Type ID | protease017976 |
| Protein Name |
ATP-dependent Clp protease proteolytic subunit, mitochondrial EC 3.4.21.92 Endopeptidase Clp |
| Gene Name | CLPP |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MWPGILVGGARVASCRYPALGPRLAAHFPAQRPPQRTLQNGLALQRCLHATATRALPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPTLVQKEPVEAAPAAEPVPAST |
| Enzyme Length | 277 |
| Uniprot Accession Number | Q16740 |
| Absorption | |
| Active Site | ACT_SITE 153; /note=Nucleophile; /evidence=ECO:0000269|PubMed:11923310; ACT_SITE 178; /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:0000269|PubMed:11923310, ECO:0000269|PubMed:15522782, ECO:0000269|PubMed:22354088}; |
| 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 (PubMed:11923310, PubMed:15522782). Cleaves PINK1 in the mitochondrion (PubMed:22354088). {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:15522782, ECO:0000269|PubMed:22354088}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (11); Chain (1); Helix (7); Modified residue (2); Mutagenesis (2); Natural variant (3); Region (1); Sequence conflict (1); Transit peptide (1) |
| Keywords | 3D-structure;Acetylation;Deafness;Direct protein sequencing;Disease variant;Hydrolase;Mitochondrion;Protease;Reference proteome;Serine protease;Transit peptide |
| Interact With | Q9NYB9-2; P05067; P54252; Q9NWQ9; P50570-2; Q86UW9; Q12805; O95967; Q8TB36; P28799; P42858; Q8WXH2; P61970; Q7Z4N8; Q9NRQ2; P67775; P20618; Q93062-3; P37840; Q13148; Q9Y5L0; O76024; O76031 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:10525407, ECO:0000269|PubMed:22354088}. |
| Modified Residue | MOD_RES 200; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:O88696; MOD_RES 211; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1TG6; 6BBA; 6DL7; 6H23; |
| Mapped Pubmed ID | 17353931; 18378094; 20877624; 21911578; 23360988; 25083874; 26058080; 26606371; 26675528; 26970254; 27087618; 27154400; 27389535; 28449241; 30126533; 30129683; 30877431; 30878663; 31056398; 32342250; 32399598; 34207660; 34943861; |
| Motif | |
| Gene Encoded By | |
| Mass | 30,180 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.92; |