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Literature summary for 3.4.21.B30 extracted from
- Subunit-specific degradation of the UmuD/D' heterodimer by the ClpXP protease: the role of trans recognition in UmuD' stability (2000), EMBO J., 19, 5251-5258.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| F26A/P27A/S28A/P29A | can form heterodimers and is recognized by ClpXP protease | Escherichia coli |
| L9A/R10A/E11A/I12A | heterodimer with UmuD' displays a significant increase in stability | Escherichia coli |
General Stability
| General Stability | Organism |
|---|---|
| highly purified UmuD/D' heterodimer is degraded in the presence of ATP, ClpP and ClpX, no degradation occurs when ClpX is omitted | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | inactive UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD' | Escherichia coli |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | although UmuD and UmuD' form homodimers, they preferentially form heterodimers, SDS-PAGE | Escherichia coli |
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