EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.21.92 | Phe-Ala-Pro-His-Met-Ala-Leu-Val-Pro-Val + H2O |
synthetic polypeptide that corresponds to the 10 amino acids surrounding the in vivo processing site in ClpP subunit |
Escherichia coli |
? |
- |
? |
| 3.4.21.92 | stalk synthesis transcription factor TacA + H2O |
TacA degradation is controlled during the cell cycle dependent on the ClpXP regulator CpdR and stabilization of TacA increases degradation of another ClpXP substrate, CtrA, while restoring deficiencies associated with prolific CpdR activity |
Caulobacter vibrioides |
? |
- |
? |
| 3.4.21.92 | more |
the ClpP N-terminus acts as a gate controlling substrate access to the active sites, binding of ClpA opens this gate, allowing substrate entry and formation of the acyl-enzyme intermediate, and closing of the N-terminal gate stimulates acyl-enzyme hydrolysis |
Escherichia coli |
? |
- |
? |
| 3.4.21.92 | Starvation proteins + H2O |
the ClpP proteolytic subunit plays a subtle but important role when cells are recovering from starvation. This enzyme is important in the selective degradation of starvation proteins when growth resumes |
Escherichia coli |
? |
- |
? |
| 3.4.21.92 | more |
the high degree of similarity among the ClpA-like proteins suggests that Clp-like proteases are likely to be important participants in energy-dependent proteolysis in prokaryotic and eukaryotic cells |
Escherichia coli |
? |
- |
? |
| 3.4.21.92 | more |
the high degree of similarity among the ClpA-like proteins suggests that Clp-like proteases are likely to be important participants in energy-dependent proteolysis in prokaryotic and eukaryotic cells |
Escherichia coli CSH100 (ClpA) |
? |
- |
? |
| 3.4.21.92 | more |
the SsrA tag directs proteins to degradation by both ClpP1 and ClpP2. The terminal three residues of the ssrA-tag sequence are LAA. A LAA-tag is sufficient to direct proteins into the degradation pathway |
Mycobacterium tuberculosis |
? |
- |
? |
| 3.4.21.92 | more |
the SsrA tag directs proteins to degradation by both ClpP1 and ClpP2. The terminal three residues of the ssrA-tag sequence are LAA. A LAA-tag is sufficient to direct proteins into the degradation pathway |
Mycobacterium tuberculosis H37Rv |
? |
- |
? |
| 3.4.21.92 | N-succinyl-Ile-Ile-Trp-7-amido-4-methylcoumarin + H2O |
throughout the 5 min time course, ClpP readily degrades the dipeptide, whereas ClpP3/R does not. Prolonging the incubation time with ClpP3/R to 20 min does not result in any visible degradation. Addition of ClpC to the assays also fails to produce any degradation |
Synechococcus elongatus |
N-succinyl-Ile-Ile-Trp + 7-amino-4-methylcoumarin |
- |
? |
| 3.4.21.92 | N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O |
throughout the 5 min time course, ClpP readily degrades the dipeptide, whereas ClpP3/R does not. Prolonging the incubation time with ClpP3/R to 20 min does not result in any visible degradation. Addition of ClpC to the assays also fails to produce any degradation |
Synechococcus elongatus |
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin |
- |
? |
