3.4.21.B30	additional information	binds to a cleft located between two RecA monomers in the crystal structure	
3.4.21.B30	additional information	enzyme interacts with RecA	
3.4.21.B30	additional information	interacts with RecA protein	
3.4.21.B30	additional information	interacts with RecA-DNA filament and participates in mutagenesis	
3.4.21.B30	additional information	role in mutagenesis	
3.4.21.B30	additional information	role in SOS mutagenesis	
3.4.21.B30	additional information	role in UV mutagenesis	
3.4.21.B30	additional information	UmuD and UmuD' interact differently with polymerase III: whereas uncleaved UmuD interacts more strongly with beta than it does with alpha, UmuD' interacts more strongly with alpha than with beta	
3.4.21.B30	additional information	UmuD' protein is a component of DNA polymerase V	
3.4.21.B30	additional information	UmuD' protein is a component of DNA polymerase V, role in translesion DNA synthesis	
3.4.21.B30	additional information	the damage-induced RecA:ssDNA nucleoprotein filament facilitates autocleavage of the N-terminal 24-amino acids of UmuD2 to yield UmuD'2, the form that enables mutagenesis	
3.4.21.B30	additional information	UmuD2 undergoes autodigestion at elevated pH	
3.4.21.B30	additional information	enzyme UmuD does not bind DNA. the enzyme UmuD interacts with several components of DNA polymerase III, including the polymerase subunit alpha, the beta clamp and the proofreading subunit epsilon, homology modeling and protein-protein docking analysis, overview. It interacts with the alpha subunit of DNA polymerase III at two distinct binding sites, one of which is adjacent to the single-stranded DNA-binding site. Enzyme UmuD specifically inhibits binding of DNA polymerase III alpha to ssDNA, UmuD residues D91 and G92 are involved in this interaction, molecular modeling, overview	
3.4.21.B30	UmuD + H2O	auto-cleavage of UmuD to UmuD'	
3.4.21.B30	UmuD2 + H2O	slow auto-cleavage of UmuD2 to UmuD'2	
3.4.21.B30	UmuDAb + H2O	slow auto-cleavage of UmuDAb to UmuDAb'. UmuDAb undergoes a post-translational, LexA-like cleavage event after DNA damage, possibly to achieve its regulatory action