Detail Information for IndEnz0002017079
IED ID IndEnz0002017079
Enzyme Type ID protease017079
Protein Name ATP-dependent Clp protease proteolytic subunit 1, mitochondrial
EC 3.4.21.92
Gene Name clpp-1 CBG00853
Organism Caenorhabditis briggsae
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis briggsae
Enzyme Sequence MLRRILTTSSVRNLTSSTQARVGIPFVIDNEGKGERTYDIYSRLLRDRIVCLMTPVDDFMASALIAQLLFLQSESSKKPIHMYINSPGGSVTAGLAIYDTMQMISAPVATWVIGQASSMGSLLLAAGEKGMRSALPNARIMVHQPSGGAQGTCSDIVIRAEEITRLKKRLNEIYVHHTGISYDEIERTLDRDRFMSAQEALKFGLVDKIEKHTGSMPTD
Enzyme Length 219
Uniprot Accession Number A8WPG6
Absorption
Active Site ACT_SITE 118; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 143; /evidence=ECO:0000255
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:0000255};
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 (By similarity). {ECO:0000250|UniProtKB:Q27539}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Transit peptide (1)
Keywords Hydrolase;Mitochondrion;Protease;Reference proteome;Serine protease;Transit peptide
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q27539}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 24,150
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda