3.4.21.B30	proteolytic modification	full-length UmuD is expressed as a homodimer of 139-amino-acid subunits, which eventually cleaves its N-terminal 24 amino acids to form UmuD'. The cleavage product UmuD' and UmuC form the Y-family polymerase DNA Pol V (UmuD'2C) capable of performing translesion synthesis	-, 752775	
3.4.21.B30	proteolytic modification	inactive form UmuD is cleaved into active form UmuD'	651628	
3.4.21.B30	proteolytic modification	inactive UmuD is posttranslationally activated by a RecA-mediated cleavage at its Gys24-Gly25 bond that yields UmuD', UmuD monomer is a better substrate for the cleavage reaction than the dimer	651630	
3.4.21.B30	proteolytic modification	inactive UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD'	650976, 653236	
3.4.21.B30	proteolytic modification	inactive UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD', P67D and P67R mutations of RecA result in reduced UmuD cleavage	652778	
3.4.21.B30	proteolytic modification	processing of UmuD to the shorter, but mutagenically active UmuD' by activated RecA	653602	
3.4.21.B30	proteolytic modification	processing of UmuD to the shorter, but mutagenically active UmuD' by ClpXP protease, UmuD' must form a heterodimer with its unabbreviated precursor for efficient degradation, UmuD2 homodimers are degraded with an efficiency similar to the UmuD' subunit of the UmuD/UmuD' heterodimer	653588	
3.4.21.B30	proteolytic modification	RecA-facilitated cleavage of UmuD to UmuD' can be inhibited by overexpression of polymerase III subunits that interact with UmuD	653620	
3.4.21.B30	proteolytic modification	RecA-facilitated cleavage of UmuD yields a carboxy-terminal fragment UmuD' that is active for mutagenesis, no other SOS gene products other than activated RecA are required for UmuD processing, high levels of activated RecA are required for cleavage in vivo	653235	
3.4.21.B30	proteolytic modification	RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD'	652782	
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