| IED ID | IndEnz0002016492 |
| Enzyme Type ID | protease016492 |
| Protein Name |
ATP-dependent Clp protease proteolytic subunit EC 3.4.21.92 Caseinolytic protease Endopeptidase Clp Heat shock protein F21.5 Protease Ti |
| Gene Name | clpP lopP b0437 JW0427 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MSYSGERDNFAPHMALVPMVIEQTSRGERSFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIYLYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGKRFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQSLEQIERDTERDRFLSAPEAVEYGLVDSILTHRN |
| Enzyme Length | 207 |
| Uniprot Accession Number | P0A6G7 |
| Absorption | |
| Active Site | ACT_SITE 111; /note=Nucleophile; /evidence=ECO:0000305; ACT_SITE 136; /evidence=ECO:0000305; ACT_SITE 185; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by benzyloxycarbonyl leucyltyrosine chloromethylketone (Z-LY-CMK). {ECO:0000269|PubMed:16682229}. |
| 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|HAMAP-Rule:MF_00444}; |
| 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE (PubMed:24375411). {ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:12941278, ECO:0000269|PubMed:15371343, ECO:0000269|PubMed:24375411}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (14); Chain (1); Helix (7); Mutagenesis (12); Propeptide (1); Turn (2) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Serine protease;Stress response;Zymogen |
| Interact With | P0ABH9; Itself; P0A6H1 |
| Induction | INDUCTION: By heat shock. Part of the clpP-clpX operon. {ECO:0000269|PubMed:8093059}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (13); X-ray crystallography (7) |
| Cross Reference PDB | 1TYF; 1YG6; 1YG8; 2FZS; 3HLN; 3MT6; 6NB1; 6PO1; 6PO3; 6POD; 6POS; 6PPE; 6UQE; 6UQO; 6W1Z; 6W20; 6W21; 6WR2; 6WRF; 6WSG; |
| Mapped Pubmed ID | 15004283; 15690043; 16606699; 16858726; 1783205; 19183285; 19317833; 24049175; 24561554; 24627523; 26058080; 32108573; 32313240; 33089779; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,187 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 mM for N-succinyl-Leu-Tyr-7-amino-4-methyl-coumarin (N-succinyl-Leu-Tyr-AMC) {ECO:0000269|PubMed:16406682, ECO:0000269|PubMed:20637416}; KM=1.0 mM for N-succinyl-Leu-Tyr-AMC {ECO:0000269|PubMed:16406682, ECO:0000269|PubMed:20637416}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.92; |