IED ID | IndEnz0002004520 |
Enzyme Type ID | protease004520 |
Protein Name |
ATP-dependent Clp protease proteolytic subunit EC 3.4.21.92 Endopeptidase Clp Cleaved into: Ceu clpP intein Insertion IS2 |
Gene Name | clpP |
Organism | Chlamydomonas moewusii (Chlamydomonas eugametos) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Chlorophyta core chlorophytes Chlorophyceae CS clade Chlamydomonadales Chlamydomonadaceae Chlamydomonas Chlamydomonas moewusii (Chlamydomonas eugametos) |
Enzyme Sequence | MPIGVPRIIYCWGEELPAQWTDIYNFIFRRRMVFLMQYLDDELCNQICGLLINIHMEDRSKELEKKEIERSGLFKGGPKTQKGGTGAGETGASSIQNKKSNSSSFEDLLAADEDLGIDENNTLEQYTLQKITMEWLNWNAQFFDYSDEPYLFYLAEMLSKDFNKGDARMLFSNNNKFSMPFSQMLNTGSMSDPRRPQSTNGANWNSSEQNNSLDIYSPFRMLANFEAQDYDFKQINPSLASKEEVFKLFNNTILKNGGQRNNNMSKLLTELAQRNWENKTNSQENLYKSTEKALSQRNLRKEYIKDRTLNNYSSDPFNTKGYVNAQGASTGPSPRTRGMHADGSLNYLDFYSYNDSYNDFKTAPRGKQAERAFQEEESKKVFVIINSFGGSVGNGITVHDALQFIKAGSLTLALGVAASAASLALAGGTIGERYVTEGCHVMIHQPECLTSDHTVLTTRGWIPIADVTLDDKVAVLDNNTGEMSYQNPQKVHKYDYEGPMYEVKTAGVDLFVTPNHRMYVNTTNNTTNQNYNLVEASSIFGKKVRYKNDAIWNKTDYQFILPETATLTGHTNKISSTPAIQPEMNAWLTFFGLWIANGHTTKIAEKTAENNQQKQRYKVILTQVKEDVCDIIEQTLNKLGFNFIRSGKDYTIENKQLWSYLNPFDNGALNKYLPDWVWELSSQQCKILLNSLCLGNCLFTKNDDTLHYFSTSERFANDVSRLALHAGTTSTIQLEAAPSNLYDTIIGLPVEVNTTLWRVIINQSSFYSYSTDKSSALNLSNNVACYVNAQSALTLEQNSQKINKNTLVLTKNNVKSQTMHSQRAERVDTALLTQKELDNSLNHEILINKNPGTSQLECVVNPEVNNTSTNDRFVYYKGPVYCLTGPNNVFYVQRNGKAVWTGNSSIQGQASDIWIDSQEIMKIRLDVAEIYSLATYRPRHKILRDLDRDFYLTATETIHYGLADEIASNEVMQEIIEMTSKVWDYHDTKQQRLLESRDSTTSGADTQSQN |
Enzyme Length | 1010 |
Uniprot Accession Number | P42379 |
Absorption | |
Active Site | ACT_SITE 419; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10085, ECO:0000255|PROSITE-ProRule:PRU10086"; ACT_SITE 444; /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; Evidence={ECO:0000255|PROSITE-ProRule:PRU10085, ECO:0000255|PROSITE-ProRule:PRU10086}; |
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 (3); Compositional bias (1); Domain (1); Region (3) |
Keywords | Autocatalytic cleavage;Chloroplast;Hydrolase;Plastid;Protease;Protein splicing;Serine protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | Chloroplast |
Mass | 114,552 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.21.92; |