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; |