Detail Information for IndEnz0002005486
IED ID IndEnz0002005486
Enzyme Type ID protease005486
Protein Name ATP-dependent Clp protease proteolytic subunit
EC 3.4.21.92
Endopeptidase Clp
Gene Name clpP
Organism Chloranthus spicatus (Chulantree) (Nigrina spicata)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Chloranthales Chloranthaceae Chloranthus Chloranthus spicatus (Chulantree) (Nigrina spicata)
Enzyme Sequence MPIGVPKVPFRSPGEEDAVWVDVNRLHRERLLFLGQEVDSEISNQLVGLMVYLSIEDDTRDLYLFINSPGGWVIPGLTIYDTMQFVPPDVHTICMGLAASMGSFILVGGEITKRLAFPHARIMIHQPASSFYEAQAGEFILEAEELLKLRETLTRVYVQRTGNPLWIVSEDMERDVFMSATEAQAHGIVDLVAVENTGDFA
Enzyme Length 201
Uniprot Accession Number A6MME7
Absorption
Active Site ACT_SITE 100; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_00444; ACT_SITE 125; /evidence=ECO:0000255|HAMAP-Rule:MF_00444
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|HAMAP-Rule:MF_00444};
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. {ECO:0000255|HAMAP-Rule:MF_00444}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1)
Keywords Chloroplast;Hydrolase;Plastid;Protease;Serine protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000255|HAMAP-Rule:MF_00444}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By Chloroplast
Mass 22,468
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda