| IED ID | IndEnz0002018430 |
| Enzyme Type ID | protease018430 |
| Protein Name |
ATP-dependent Clp protease proteolytic subunit EC 3.4.21.92 Caseinolytic protease Endopeptidase Clp Stress protein G7 |
| Gene Name | clpP yvdN BSU34540 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MNLIPTVIEQTNRGERAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFLAAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTICIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQGQATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDRDNFKSAEEALEYGLIDKILTHTEDKK |
| Enzyme Length | 197 |
| Uniprot Accession Number | P80244 |
| Absorption | |
| Active Site | ACT_SITE 98; /note="Nucleophile"; /evidence="ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375"; ACT_SITE 123; /evidence="ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375" |
| Activity Regulation | ACTIVITY REGULATION: Low intrinsic peptidase activity is stimulated by ATP-binding subunits ClpC, ClpE and ClpX. Activity is disregulated by acyldepsipeptides (ADEP) antibiotics, which negate the need for ATP-binding subunits for activation and which makes it into an unregulated protease. Each ClpP subunit binds 1 ADEP molecule, which prevents binding of ClpX. ADEP binding causes conformational shifts that open the gated pore of the ring (PubMed:20305655). Protease activity is inhibited by diisopropylfluoro-phosphate (PubMed:22080375). Protease activity is inhibited by bortezomib, an oncology drug originally designed to work on the human proteasome (PubMed:31155236). {ECO:0000269|PubMed:20305655, ECO:0000269|PubMed:22080375, ECO:0000269|PubMed:31155236}. |
| 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, ECO:0000269|PubMed:20305655}; |
| 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 limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX (PubMed:20305655). Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor (PubMed:16899079). Probably the major protease that degrades proteins tagged by trans-translation (PubMed:11395451, PubMed:31155236). {ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:11395451, ECO:0000269|PubMed:16899079, ECO:0000269|PubMed:20305655, ECO:0000269|PubMed:31155236}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (10); Chain (1); Helix (7); Mutagenesis (8) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Serine protease;Stress response |
| Interact With | Itself |
| Induction | INDUCTION: By heat shock, salt stress, ethanol stress, oxidative stress, glucose limitation and oxygen limitation. {ECO:0000269|PubMed:1362210, ECO:0000269|PubMed:8012595, ECO:0000269|PubMed:9643546}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 3KTG; 3KTH; 3KTI; 3KTJ; 3KTK; 3TT6; 3TT7; |
| Mapped Pubmed ID | 16525504; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,682 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.92; |