Detail Information for IndEnz0002017083
IED ID IndEnz0002017083
Enzyme Type ID protease017083
Protein Name ATP-dependent Clp protease proteolytic subunit 1, mitochondrial
EC 3.4.21.92
Endopeptidase Clp
Gene Name clpp-1 ZK970.2
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MLRRLVTSSLSASRSMSASVQSRVGIPFVIDNEGKGERTYDIYSRLLRDRIVCLMTPVDDFIASALIAQLLFLQSESGKKPIHMYINSPGGSVTAGLAIYDTIQMISAPVSTWVIGQASSMGSLLLCAGEKGMRSALPNSRIMVHQPSGGAQGTCSDIVIRAEEITRLKRRLNEIYVHHTGMSYDEIEKTLDRDRFMSAHEALKFGLVDQIETHNGSMPSD
Enzyme Length 221
Uniprot Accession Number Q27539
Absorption
Active Site ACT_SITE 120; /note=Nucleophile; /evidence=ECO:0000305; ACT_SITE 145; /evidence=ECO:0000305
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;
DNA Binding
EC Number 3.4.21.92
Enzyme Function FUNCTION: Clp cleaves peptides in various proteins in a process that requires ATP hydrolysis. Clp may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. {ECO:0000269|PubMed:17925224}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (2); Chain (1); Transit peptide (1)
Keywords Alternative splicing;Hydrolase;Mitochondrion;Protease;Reference proteome;Serine protease;Transit peptide
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:17925224}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 14551910; 15791247; 17486083; 17704769; 18082681; 20188671; 21085631; 21177967; 22286215; 22560298; 23800452; 25487147; 26913604; 27133166; 27457958; 27610575;
Motif
Gene Encoded By
Mass 24,266
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.92;