3.4.21.B30: UmuD protein
This is an abbreviated version!
For detailed information about UmuD protein, go to the full flat file.
Word Map on EC 3.4.21.B30
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3.4.21.B30
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reca
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translesion
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mucab
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polymerases
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damage-induced
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uv-induced
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reca-mediated
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mutable
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mutability
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umud\'c
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transversions
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error-free
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sos-induced
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abasic
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sos-regulated
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self-cleavage
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replication-blocking
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n-2-acetylaminofluorene
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reca430
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sos-independent
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y-family
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at->ta
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lexadef
- 3.4.21.B30
- reca
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translesion
-
mucab
- polymerases
-
damage-induced
-
uv-induced
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reca-mediated
-
mutable
-
mutability
-
umud\'c
-
transversions
-
error-free
-
sos-induced
-
abasic
-
sos-regulated
-
self-cleavage
-
replication-blocking
-
n-2-acetylaminofluorene
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reca430
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sos-independent
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y-family
-
at->ta
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lexadef
Reaction
involved in UV protection and mutation. Essential for induced (or SOS) mutagenesis. May modify the DNA replication machinery to allow bypass synthesis across a damaged template =
Synonyms
DNA damage response protein, error-prone polymerase accessory, ImpA, MucA, polymerase manager protein UmuD, RulA, S24.003, SamA, UmuD, UmuD', UmuD2, UmuDAb, UmuDC, umuDpR, UmuDpR protein, UmuD’2
ECTree
3.4.21.B30 UmuD proteinAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.21.B30 - UmuD protein
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UmuDAb + H2O
UmuDAb' + ?
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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
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?
additional information
?
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binds to a cleft located between two RecA monomers in the crystal structure
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?
additional information
?
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interacts with RecA-DNA filament and participates in mutagenesis
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?
additional information
?
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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
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?
additional information
?
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UmuD' protein is a component of DNA polymerase V
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?
additional information
?
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UmuD' protein is a component of DNA polymerase V, role in translesion DNA synthesis
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?
additional information
?
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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
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?
additional information
?
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UmuD2 undergoes autodigestion at elevated pH
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?
additional information
?
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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
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