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Literature summary for 3.4.21.92 extracted from

  • Lee, M.E.; Baker, T.A.; Sauer, R.T.
    Control of substrate gating and translocation into ClpP by channel residues and ClpX binding (2010), J. Mol. Biol., 399, 707-718.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Escherichia coli

Protein Variants

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
ClpP
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Escherichia coli