Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ClpX | ClpX binding stimulates ClpP cleavage of peptides larger than a few amino acids and enhances ClpP active-site modification. Stimulation requires ATP binding but not hydrolysis by ClpX | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
Delta1-10 | deletion of the N-terminal 10, 14, or 17 residues of mature ClpP allows these mutants to degrade alpha-casein, a natively unfolded protein | Escherichia coli |
DELTA1-14 | deletion of the N-terminal 10, 14, or 17 residues of mature ClpP allows these mutants to degrade alpha-casein, a natively unfolded protein | Escherichia coli |
DELTA1-17 | deletion of the N-terminal 10, 14, or 17 residues of mature ClpP allows these mutants to degrade alpha-casein, a natively unfolded protein | Escherichia coli |
E8A/R12A/E14A/R15A | residues 8-15 form the channel loop of the pore: when charged residues in the channel (amino acids 8-15) are changed with alanine this mutant cleaves the decapeptide at a rate 8fold faster than observed with wild-type ClpP but cleaves the dipeptide at a comparable rate. Mutant shows a substantial GFP-ssrA degradation similar to wild-type | Escherichia coli |
E8G/Q9G/T10G/S11G/R12G/G13G/E14G/R15G | residues 8-15 form the channel loop of the pore: when replaced with eight glycines this mutant cleaves the decapeptide at a rate 8fold faster than observed with wild-type ClpP but cleaves the dipeptide at a comparable rate. Mutant shows a much slower degradation of GFP-ssrA | Escherichia coli |
E8G/R12G/E14G/R15G | residues 8-15 form the channel loop of the pore: when charged residues in the channel (amino acids 8-15) are changed with glycine this mutant cleaves the decapeptide at a rate 8fold faster than observed with wild-type ClpP but cleaves the dipeptide at a comparable rate. Mutant shows a much slower degradation of GFP-ssrA | Escherichia coli |
E8R/R12E/E14R/R15E | residues 8-15 form the channel loop of the pore: when charged residues in the channel (amino acids 8-15) are reversed this mutant cleaves the decapeptide at a rate 8fold faster than observed with wild-type ClpP but cleaves the dipeptide at a comparable rate. Mutant shows a much slower degradation of GFP-ssrA | Escherichia coli |
I19A | mutant shows wild-type level of dipeptide cleavage, 20fold increase in decapeptide cleavage compared to wild-type, in contrast to wild-type mutant degrades 113-residue unfolded I27 domain of human titin. Mutant shows high decrease in ClpX affinity | Escherichia coli |
I19D | mutant shows 16fold increase in decapeptide cleavage compared to wild-type | Escherichia coli |
I19L | mutant shows 6fold increase in decapeptide cleavage compared to wild-type | Escherichia coli |
K25A | mutant shows wild-type level of dipeptide cleavage, 1.5fold increase in decapeptide cleavage compared to wild-type. Mutant shows only moderate decrease in ClpX affinity | Escherichia coli |
L23A | mutant shows wild-type level of dipeptide cleavage, 5fold increase in decapeptide cleavage compared to wild-type. Mutant shows only moderate decrease in ClpX affinity | Escherichia coli |
L24A | mutant shows wild-type level of dipeptide cleavage, 20fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity | Escherichia coli |
R22A | mutant shows wild-type level of dipeptide cleavage, 1.5fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity | Escherichia coli |
S21A | mutant shows wild-type level of dipeptide cleavage, 5fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity | Escherichia coli |
Y20A | mutant shows wild-type level of dipeptide cleavage, 5fold increase in decapeptide cleavage compared to wild-type. Mutant shows high decrease in ClpX affinity | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | ClpP associates with ClpX or ClpA to form the AAA+ ClpXP or ClpAP proteases | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Abz-KASPVSLGY(NO2)D + H2O | - |
Escherichia coli | ? | - |
? | |
GFP-ssrA + H2O | - |
Escherichia coli | ? | - |
? | |
additional information | ClpP associates with ClpX or ClpA to form the AAA+ ClpXP or ClpAP proteases | Escherichia coli | ? | - |
? | |
succinyl-LY-4-methylcoumarin-7-amide + H2O | - |
Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ClpP | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Escherichia coli |