Detail Information for IndEnz0002018198
IED ID IndEnz0002018198
Enzyme Type ID protease018198
Protein Name Putative ATP-dependent Clp protease proteolytic subunit
EC 3.4.21.92
Endopeptidase Clp
PS7/PS12
Fragments
Gene Name clpP
Organism Pinus strobus (Eastern white pine)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Acrogymnospermae Pinopsida Pinidae Conifers I Pinaceae Pinus Pinus subgen. Strobus Pinus strobus (Eastern white pine)
Enzyme Sequence APTEADATWVDLYNRVMIHQPASSYYAAEMHNEAKTDNPEEVLDLDRDVFMSAAYGIVDTVWYVQAELVNGRGGAVVAGL
Enzyme Length 80
Uniprot Accession Number P84723
Absorption
Active Site ACT_SITE 19; /evidence="ECO:0000255|PROSITE-ProRule:PRU10085, ECO:0000255|PROSITE-ProRule:PRU10086"
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:Q85X43, ECO:0000255|PROSITE-ProRule:PRU10085, ECO:0000255|PROSITE-ProRule:PRU10086};
DNA Binding
EC Number 3.4.21.92
Enzyme Function FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). {ECO:0000250|UniProtKB:Q85X43}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Non-adjacent residues (7); Non-terminal residue (2)
Keywords Chloroplast;Direct protein sequencing;Hydrolase;Plastid;Protease;Serine protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 8,790
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda