Detail Information for IndEnz0002018137
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;