Detail Information for IndEnz0002017976
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;