UniProt functional annotation for P0A6G7



	UniProt functional annotation for P0A6G7

UniProt code: P0A6G7.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

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}.

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};

Activity regulation: Inhibited by benzyloxycarbonyl leucyltyrosine chloromethylketone (Z-LY-CMK). {ECO:0000269|PubMed:16682229}.

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};

Subunit: Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. Component of the ClpAP and ClpXP complexes. {ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000269|PubMed:16406682, ECO:0000269|PubMed:16682229, ECO:0000269|PubMed:20637416, ECO:0000269|PubMed:20851345, ECO:0000269|PubMed:9390554}.

Subcellular location: Cytoplasm.

Induction: By heat shock. Part of the clpP-clpX operon. {ECO:0000269|PubMed:8093059}.

Domain: The N-terminus (residues 17-34) interact with ClpA and ClpX. {ECO:0000269|PubMed:16406682}.

Disruption phenotype: Cells undergo an apoptotic-like death upon DNA damage characterized by membrane depolarization (PubMed:22412352). Decreased persister cell formation upon antibiotic challenge probably due to increased levels of MazF toxin (PubMed:24375411). {ECO:0000269|PubMed:22412352, ECO:0000269|PubMed:24375411}.

Miscellaneous: Acyldepsipeptide antibiotics bind in the ClpA or ClpX binding-sites, rendering the enzyme ATP-independent and indiscriminate, thus killing cells. {ECO:0000305|PubMed:20851345}.

Similarity: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP- Rule:MF_00444}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



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}.


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};
Activity regulation:		Inhibited by benzyloxycarbonyl leucyltyrosine chloromethylketone (Z-LY-CMK). {ECO:0000269\|PubMed:16682229}.
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};
Subunit:		Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. Component of the ClpAP and ClpXP complexes. {ECO:0000255\|HAMAP-Rule:MF_00444, ECO:0000269\|PubMed:16406682, ECO:0000269\|PubMed:16682229, ECO:0000269\|PubMed:20637416, ECO:0000269\|PubMed:20851345, ECO:0000269\|PubMed:9390554}.
Subcellular location:		Cytoplasm.
Induction:		By heat shock. Part of the clpP-clpX operon. {ECO:0000269\|PubMed:8093059}.
Domain:		The N-terminus (residues 17-34) interact with ClpA and ClpX. {ECO:0000269\|PubMed:16406682}.
Disruption phenotype:		Cells undergo an apoptotic-like death upon DNA damage characterized by membrane depolarization (PubMed:22412352). Decreased persister cell formation upon antibiotic challenge probably due to increased levels of MazF toxin (PubMed:24375411). {ECO:0000269\|PubMed:22412352, ECO:0000269\|PubMed:24375411}.
Miscellaneous:		Acyldepsipeptide antibiotics bind in the ClpA or ClpX binding-sites, rendering the enzyme ATP-independent and indiscriminate, thus killing cells. {ECO:0000305\|PubMed:20851345}.
Similarity:		Belongs to the peptidase S14 family. {ECO:0000255\|HAMAP- Rule:MF_00444}.