EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.B30 | proteolytic modification |
RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD', K232A/E235A mutant of RecA cleaves UmuD more efficiently than wild-type RecA, T242A/R234A mutant of RecA is defective for cleavage of UmuD |
651650 |
| 3.4.21.B30 | proteolytic modification |
RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD', Salmonella typhimurium UmuD is processed at a significantly faster rate than the Escherichia coli protein, enhanced cleavage can be attributed to the presence of a Pro23 residue |
652782 |
| 3.4.21.B30 | proteolytic modification |
slow auto-cleavage of UmuD2 to UmuD'2, the heterodimer efficiently cleaves to form UmuD'2 |
-, 731345 |
| 3.4.21.B30 | proteolytic modification |
UmuD is expressed as a 139-amino-acid protein, which eventually cleaves its N-terminal 24 amino acids to form UmuD'. Cleavage of UmuD to UmuD' dramatically affects the function of the protein and activates UmuC for translesion synthesis by forming DNA Polymerase V |
-, 755139 |
| 3.4.21.B30 | proteolytic modification |
UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD' |
653604 |
| 3.4.21.B30 | proteolytic modification |
UmuD is posttranslationally activated by cleavage yielding UmuD' |
651420 |
| 3.4.21.B30 | proteolytic modification |
UmuD protein is activated by a RecA-single-stranded DNA-facilitated self-cleavage event that serves to remove its amino-terminal 24 residues to yield UmuD' |
651685 |
