Detail Information for IndEnz0002018374
IED ID IndEnz0002018374
Enzyme Type ID protease018374
Protein Name ATP-dependent Clp protease proteolytic subunit 5, chloroplastic
EC 3.4.21.92
Endopeptidase ClpP5
nClpP5
nClpP1
Gene Name CLPP5 NCLPP1 NCLPP5 At1g02560 T14P4.12
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MAHACVSTSASSLRFTAGFVSASPNGSSFDSPKLSLPFEPLRSRKTNKLVSDRKNWKNSTPKAVYSGNLWTPEIPSPQGVWSIRDDLQVPSSPYFPAYAQGQGPPPMVQERFQSIISQLFQYRIIRCGGAVDDDMANIIVAQLLYLDAVDPTKDIVMYVNSPGGSVTAGMAIFDTMRHIRPDVSTVCVGLAASMGAFLLSAGTKGKRYSLPNSRIMIHQPLGGAQGGQTDIDIQANEMLHHKANLNGYLAYHTGQSLEKINQDTDRDFFMSAKEAKEYGLIDGVIMNPLKALQPLAAA
Enzyme Length 298
Uniprot Accession Number Q9S834
Absorption
Active Site ACT_SITE 193; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 218; /evidence=ECO:0000250
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: 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}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Modified residue (1); Sequence conflict (6); Transit peptide (1)
Keywords Acetylation;Chloroplast;Direct protein sequencing;Hydrolase;Plastid;Protease;Reference proteome;Serine protease;Transit peptide;Ubl conjugation
Interact With
Induction INDUCTION: Repressed in darkness. Induced by high light stress and during cold acclimation (at protein level). {ECO:0000269|PubMed:10427773, ECO:0000269|PubMed:11982939}.
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:11982939, ECO:0000269|PubMed:14593120}.
Modified Residue MOD_RES 101; /note=N-acetylglycine; /evidence=ECO:0007744|PubMed:22223895
Post Translational Modification PTM: Ubiquitinated in vitro by CHIP. {ECO:0000269|PubMed:26085677}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12185496; 12766230; 12938931; 14576160; 15829605; 15998247; 16207701; 16648217; 16895613; 17181860; 17932292; 18297659; 18431481; 18633119; 21139083; 23548781; 27247031; 28627464; 31334862; 32663165;
Motif
Gene Encoded By
Mass 32,356
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda