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Literature summary for 3.4.21.107 extracted from
- Assemblies of DegP underlie its dual chaperone and protease function (2009), FEMS Microbiol. Lett., 296, 143-148.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| cardiolipin | enhances DegP proteolytic activity at high temperatures | Escherichia coli K-12 |  |
| phosphatidyl glycerol | enhances DegP proteolytic activity at high temperatures | Escherichia coli K-12 | |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S210A | proteolytically inactive | Escherichia coli K-12 |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | - |
Escherichia coli K-12 | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| outer membrane protein + H2O | Escherichia coli K-12 | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli K-12 | P0C0V0 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| outer membrane protein + H2O | - |
Escherichia coli K-12 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homooligomer | DegP of Escherichia coli assembles into large homooligomers with an internal cavity combining both chaperone and protease activity | Escherichia coli K-12 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DegP | - |
Escherichia coli K-12 |
| HtrA | - |
Escherichia coli K-12 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | DegP is a periplasmic heat-shock protein and a key component of protein quality control in the bacterial envelope. DegP along with the Skp chaperone functions to rescue outer membrane proteins that escape recognition by SurA. At temperatures below 28°C, DegP is able to protect misfolded proteins from forming aggregates, whereas at temperatures above 30°C, misfolded proteins are efficiently degraded by DegP | Escherichia coli K-12 |
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