3.4.21.B30	malfunction	effects of recA and umuD mutations on UmuDAb cleavage in DNA damage response of Escherichia coli	731823	
3.4.21.B30	malfunction	for cleavage to occur, UmuD S60A and UmuD G25D mutant dimers must first exchange in the presence of RecA:ssDNA, and any cleavage detected results from cleavage in trans. Cleavage is less efficient in this context, indicating that the decreased rate of cleavage in the trans dimers results from the time required for dimer exchange to first take place before cleavage can occur	-, 731345	
3.4.21.B30	metabolism	competition between enzyme UmuD and ssDNA for DNA polymerase III alpha binding is a distinct mechanism for polymerase exchange	732588	
3.4.21.B30	additional information	Acinetobacter UmuDAb possesses both the conserved serine-lysine catalytic dyad required by UmuD, LexA, and some bacteriophage repressors for self-cleavage as well as the (Ala/Cys)-Gly cleavage site	731823	
3.4.21.B30	additional information	intermolecular mechanism of UmuD self-cleavage of enzyme dimers, overview	731823	
3.4.21.B30	additional information	UmuD proteins are shown to adopt multiple conformations in solution, homology models of UmuD and the structure of UmuD', overview. The heterodimer is the predominant UmuD protein conformer	-, 731345	
3.4.21.B30	physiological function	in the DNA damage response, UmuD forms part of the error-prone (UmuD'2)C polymerase V, and is activated for this function by self-cleavage after DNA damage. The umuD homologue umuDAb regulates transcription of DNA-damage induced genes. DNA damage from mitomycin C or UV exposure causes UmuDAb cleavage in both Escherichia coli wild-type and DELTAumuD cells on a timescale resembling UmuD, but does not require UmuD. UmuD and UmuDAb require RecA for cleavage	731823	
3.4.21.B30	physiological function	the active form of DNA polymerase V is UmuD'2C-RecA-ATP. RecA* transfers a single RecA-ATP stoichiometrically from its DNA 3'-end to free pol V (UmuD'2C) to form an active mutasome with the composition UmuD'2C-RecA-ATP	705887	
3.4.21.B30	physiological function	the plasmid (pUM505)-encoded UmuD homologue regulates expression of Pseudomonas aeruginosa SOS genes. The UmuDpR protein is a repressor of Pseudomonas aeruginosa SOS genes controlled by LexA	754656	
3.4.21.B30	physiological function	the protein UmuD is extensively involved in modulating cellular responses to DNA damage and may play a role in DNA polymerase exchange for damage tolerance. The polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III alpha binding to ssDNA	732588