Detail Information for IndEnz0002018344
IED ID IndEnz0002018344
Enzyme Type ID protease018344
Protein Name ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
EC 3.4.21.92
Endopeptidase ClpP3
nClpP3
nClpP4
Gene Name CLPP3 CLP NCLPP3 NCLPP4 At1g66670 F4N21.19 T12I7.12
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 MEMSLRLASSSTSNPICLLNPGKNLNFPIRNHRIPKTSKPFCVRSSMSLSKPPRQTLSSNWDVSSFSIDSVAQSPSRLPSFEELDTTNMLLRQRIVFLGSQVDDMTADLVISQLLLLDAEDSERDITLFINSPGGSITAGMGIYDAMKQCKADVSTVCLGLAASMGAFLLASGSKGKRYCMPNSKVMIHQPLGTAGGKATEMSIRIREMMYHKIKLNKIFSRITGKPESEIESDTDRDNFLNPWEAKEYGLIDAVIDDGKPGLIAPIGDGTPPPKTKVWDLWKVEGTKKDNTNLPSERSMTQNGYAAIE
Enzyme Length 309
Uniprot Accession Number Q9SXJ6
Absorption
Active Site ACT_SITE 164; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 189; /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). In the absence of CLPP3, modified ClpPR core(s) could be formed, albeit at strongly reduced levels (PubMed:23548781). {ECO:0000250, ECO:0000269|PubMed:23548781}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Modified residue (2); Region (1); Sequence conflict (3); Transit peptide (1)
Keywords Acetylation;Chloroplast;Direct protein sequencing;Hydrolase;Phosphoprotein;Plastid;Protease;Reference proteome;Serine protease;Transit peptide;Ubl conjugation
Interact With
Induction INDUCTION: Repressed in darkness. Accumulates during leaf senescence. Induced 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 71; /note=N-acetylvaline; /evidence=ECO:0007744|PubMed:22223895; MOD_RES 194; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:19376835
Post Translational Modification PTM: Ubiquitinated in vitro by CHIP. {ECO:0000269|PubMed:26085677}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12185496; 12938931; 14576160; 16207701; 16783026; 16895613; 17181860; 18431481; 24023856; 28610761; 28627464;
Motif
Gene Encoded By
Mass 33,925
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda