Detail Information for IndEnz0002018430
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;