Detail Information for IndEnz0002017572
IED ID IndEnz0002017572
Enzyme Type ID protease017572
Protein Name ATP-dependent Clp protease ATP-binding subunit CLPT2, chloroplastic
Gene Name CLPT2 CLPS2 At4g12060 F16J13.130
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 MAAHSSCNFALTNPIISQIDSFSKKKLSVPLYFFSTRKALTNPWLGVVDSSLSLTSPVSALQTNRPRRIHKSAISSLPTANPDLVVSDAKKPKWSWRAIKSFAMGELEARKLKYPNTGTEALLMGILIEGTSFTSKFLRANKIMLYKVREETVKLLGKADMYFFSPEHPPLTEDAQRALDSALDQNLKAGGIGEVMPAHILLGIWSEVESPGHKILATLGFTDEKSKELESFASESGFLDE
Enzyme Length 241
Uniprot Accession Number Q8GW78
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Accessory protein regulating the assembly of the plastidial Clp protease system (PubMed:21266658, PubMed:25921872). CLPT1 first binds to the heptameric P-ring containing the CLP3-6 subunits followed by CLPT2, and only then does the P-ring combine with the R-ring composed of the clpP1 and CLPR1-4 subunits (PubMed:21266658). Once the core complex is fully assembled, it then associates to the CLPC chaperone partner to form the functional protease (PubMed:21266658). CLPT2 and CLPT1 are partially redundant (PubMed:25921872). {ECO:0000269|PubMed:21266658, ECO:0000269|PubMed:25921872}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (1); Chain (1); Domain (1); Erroneous gene model prediction (2); Helix (9); Mutagenesis (3); Region (2); Sequence conflict (3); Transit peptide (1)
Keywords 3D-structure;Chloroplast;Plastid;Reference proteome;Repeat;Transit peptide
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:14593120, ECO:0000269|PubMed:18431481}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 4Y0C;
Mapped Pubmed ID 12185496; 12938931; 14576160; 16207701; 16766689; 16980539; 17181860; 18633119; 18650403; 28627464; 32663165;
Motif
Gene Encoded By
Mass 26,561
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda