Detail Information for IndEnz0002017551
IED ID IndEnz0002017551
Enzyme Type ID protease017551
Protein Name ATP-dependent Clp protease ATP-binding subunit CLPT1, chloroplastic
nClpC-like protein
Gene Name CLPT1 CLPS1 At4g25370 T30C3.40
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 MASYTVSFIPLTLSNPRIFVSRQNGSPSSSSRIPLTSSLLGKKLLATQPSHRCFVPKLRCLTSASTVLNVPIAQPENGSSDKIPKWSARAIKSLAMGELEARKLKYPSTGTEAILMGILVEGTSTVAKFLRGNGVTLFKVRDETLSLLGKSDMYFFSPEHPPLTEPAQKAIAWAIDEKNKSDVDGELTTAYLLLGVWSQKDSAGRQILEKLGFNEDKAKEVEKSMNEDVDLSFKKQGQ
Enzyme Length 238
Uniprot Accession Number Q93WL3
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). CLPT1 and CLPT2 are partially redundant (PubMed:25921872). {ECO:0000269|PubMed:21266658, ECO:0000269|PubMed:25921872}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (2); Chain (1); Domain (1); Erroneous gene model prediction (2); Helix (8); Mutagenesis (3); Region (2); 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:11278690, ECO:0000269|PubMed:14593120}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 4Y0B;
Mapped Pubmed ID 11826309; 12185496; 12938931; 14576160; 15028209; 16207701; 16766689; 17181860; 18431481; 18633119; 28627464; 29401302; 32663165;
Motif
Gene Encoded By
Mass 26,050
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda