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Literature summary for 3.4.21.92 extracted from
- Clp-dependent proteolysis of the LexA N-terminal domain in Staphylococcus aureus (2011), Microbiology, 157, 677-684.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| LexA N-terminal domain + H2O | - |
Staphylococcus aureus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ClpP | - |
Staphylococcus aureus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | proteolysis of the LexA N-terminal domain is dependent on ClpP. In the absence of the proteolytic subunit ClpP, or one or both of the Clp ATPases, ClpX and ClpC, the LexA domains are stabilized after autocleavage | Staphylococcus aureus |
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