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Literature summary for 3.4.21.92 extracted from
- Stepwise unfolding of a beta-barrel protein by the AAA+ ClpXP protease (2011), J. Mol. Biol., 413, 4-16.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GFP-ssrA + 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 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | ClpXP protease of Escherichia coli consists of the AAA+ ClpX unfoldase and the associated ClpP compartmental peptidase. Once the substrate is unfolded, ClpX translocates the unfolded polypeptide into the degradation chamber of ClpP in steps of five to eight amino acids per power stroke | Escherichia coli |
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Release 2023.1 (January 2023)
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