Literature summary for 3.4.21.B30 extracted from

Hare, J.M.; Adhikari, S.; Lambert, K.V.; Hare, A.E.; Grice, A.N.
The Acinetobacter regulatory UmuDAb protein cleaves in response to DNA damage with chimeric LexA/UmuD characteristics (2012), FEMS Microbiol. Lett., 334, 57-65.

Search for more literature for 3.4.21.B30

Activating Compound

Activating Compound	Comment	Organism	Structure
RecA	required for activity, RecA facilitates the intermolecular selfcleavage of UmuD2 homodimer	Escherichia coli
RecA	UmuDAb requires RecA for cleavage	Acinetobacter baylyi

Cloned(Commentary)

Cloned (Comment)	Organism
gene umuD	Escherichia coli
gene umuDAb, the umuD homologue umuDAb is present throughout the Acinetobacter genus and encodes an extra N-terminal region, transformation of Escherichia coli wild-type strain AB1157 and mutant cells with plasmids bearing various umuDAb alleles. UmuD is not required for UmuDAb expression from its native promoter, nor its disappearance after DNA damage through intermolecular interactions with Escherichia coli UmuD	Acinetobacter baylyi

Cloned (Comment)

Organism

gene umuD

Escherichia coli

gene umuDAb, the umuD homologue umuDAb is present throughout the Acinetobacter genus and encodes an extra N-terminal region, transformation of Escherichia coli wild-type strain AB1157 and mutant cells with plasmids bearing various umuDAb alleles. UmuD is not required for UmuDAb expression from its native promoter, nor its disappearance after DNA damage through intermolecular interactions with Escherichia coli UmuD

Acinetobacter baylyi

Protein Variants

Protein Variants	Comment	Organism
A83X	the site-directed mutation of UmuDAb at Ala83 abolishes cleavage activity	Acinetobacter baylyi
K156X	the site-directed mutation of UmuDAb at Lys156 abolishes cleavage activity	Acinetobacter baylyi
additional information	generation of DELTAumuD mutant cells	Escherichia coli
additional information	generation of DELTAumuD mutant cells	Acinetobacter baylyi
S119X	the site-directed mutation of UmuDAb at Ser119 abolishes cleavage activity	Acinetobacter baylyi

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
15000	-	2 * 15000, recombinant enzyme UmuD, SDS-PAGE	Escherichia coli
24000	-	x * 24000, recombinant enzyme variant UmuDAb, SDS-PAGE	Acinetobacter baylyi

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
UmuDAb + H2O	Acinetobacter baylyi	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	UmuDAb' + ?	-	?

Organism

Organism	UniProt	Comment	Textmining
Acinetobacter baylyi	-	gene umuDAb, encoded in the umuDC operon	-
Escherichia coli	-	gene umuD, encoded in the umuDC operon	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
UmuD + H2O	auto-cleavage of UmuD to UmuD'	Escherichia coli	UmuD' + ?	-	?
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' + ?	-	?
UmuDAb + H2O	slow auto-cleavage of UmuDAb to UmuDAb', cleavage site is Ala83-Gly84	Acinetobacter baylyi	UmuDAb' + ?	-	?

Subunits

Subunits	Comment	Organism
?	x * 24000, recombinant enzyme variant UmuDAb, SDS-PAGE	Acinetobacter baylyi
homodimer	2 * 15000, recombinant enzyme UmuD, SDS-PAGE	Escherichia coli

Synonyms

Synonyms	Comment	Organism
error-prone polymerase accessory	-	Escherichia coli
UmuD	-	Escherichia coli
UmuDAb	-	Acinetobacter baylyi

General Information

General Information	Comment	Organism
malfunction	effects of recA and umuD mutations on UmuDAb cleavage in DNA damage response of Escherichia coli	Escherichia coli
malfunction	effects of recA and umuD mutations on UmuDAb cleavage in DNA damage response of Escherichia coli	Acinetobacter baylyi
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	Acinetobacter baylyi
additional information	intermolecular mechanism of UmuD self-cleavage of enzyme dimers, overview	Escherichia coli
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	Acinetobacter baylyi
physiological function	when bound to UmuC, the enzyme functions as a checkpoint in delaying cell division, allowing time for error-free repair mechanisms to act, error-prone polymerase accessory UmuD. UmuD is not required for UmuDAb expression from its native promoter, nor its disappearance after DNA damage through intermolecular interactions with Escherichia coli UmuD	Escherichia coli