3.4.21.B30	additional information	binds to a cleft located between two RecA monomers in the crystal structure	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	enzyme interacts with RecA	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	interacts with RecA protein	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	interacts with RecA-DNA filament and participates in mutagenesis	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	role in mutagenesis	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	role in SOS mutagenesis	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	role in UV mutagenesis	Escherichia coli	?	-	?	89	
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	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	UmuD' protein is a component of DNA polymerase V	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	UmuD' protein is a component of DNA polymerase V, role in translesion DNA synthesis	Escherichia coli	?	-	?	89	
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	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	UmuD2 undergoes autodigestion at elevated pH	Escherichia coli	?	-	?	89	
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	Escherichia coli	?	-	?	89	
3.4.21.B30	additional information	enzyme UmuD does not bind DNA	Escherichia coli	?	-	?	89	
3.4.21.B30	UmuD + H2O	UmuD undergoes cleavage upon interaction with a RecA/ssDNA complex	Escherichia coli	?	-	?	385886	
3.4.21.B30	UmuD + H2O	auto-cleavage of UmuD to UmuD'	Escherichia coli	UmuD' + ?	-	?	431234	
3.4.21.B30	UmuD2 + H2O	autocleavage removes the N-terminal 24 amino acids of each UmuD2 to the remaining fragment UmuD2'	Escherichia coli	UmuD2' + ?	-	?	393807	
3.4.21.B30	UmuD2 + H2O	slow auto-cleavage of UmuD2 to UmuD'2	Escherichia coli	UmuD2' + ?	-	?	393807	
3.4.21.B30	UmuD2 + H2O	slow auto-cleavage of UmuD2 to UmuD'2. The wild-type UmuD homodimer cleaves in both cis and trans conformations	Escherichia coli	UmuD2' + ?	-	?	393807	
3.4.21.B30	UmuD2 + H2O	slow auto-cleavage of UmuD2 to UmuD'2	Escherichia coli AB1157	UmuD2' + ?	-	?	393807	
3.4.21.B30	UmuD2 + H2O	slow auto-cleavage of UmuD2 to UmuD'2. The wild-type UmuD homodimer cleaves in both cis and trans conformations	Escherichia coli AB1157	UmuD2' + ?	-	?	393807	
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	Acinetobacter baylyi	UmuDAb' + ?	-	?	431235	
3.4.21.B30	UmuDAb + H2O	slow auto-cleavage of UmuDAb to UmuDAb', cleavage site is Ala83-Gly84	Acinetobacter baylyi	UmuDAb' + ?	-	?	431235