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
-
translesion
-
mucab
- polymerases
-
damage-induced
-
uv-induced
-
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 (Engineering
Engineering on EC 3.4.21.B30 - UmuD protein
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A83X
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the site-directed mutation of UmuDAb at Ala83 abolishes cleavage activity
K156X
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the site-directed mutation of UmuDAb at Lys156 abolishes cleavage activity
S119X
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the site-directed mutation of UmuDAb at Ser119 abolishes cleavage activity
A31C
C24A
C25D
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site-directed mutagenesis, that removes the cleavage site Cys residue of UmuD, the mutation does not substantially affect UmuD function, cleavage site variant. For cleavage to occur, UmuD UmuD G25D dimer 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
D32C
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deficiencies in RecA-mediated cleavage as well as in UV mutagenesis, less than 30% of the wild-type activity
D3A
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the UmuD variant is non-cleavable but is a partial biological mimic of the cleaved form UmuD
D91K
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site-directed mutagenesis, the mutation abolishes the interaction between the enzyme and the DNA polymerase III alpha subunit
E35C
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deficiencies in RecA-mediated cleavage as well as in UV mutagenesis, less than 30% of the wild-type activity
F18A
decrease of induced mutagenesis to 20% of wild-type level, no cleavage of UmuD
F26A/P27A/S28A/P29A
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can form heterodimers and is recognized by ClpXP protease
G65R
G92K
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site-directed mutagenesis, the mutation abolishes the interaction between the enzyme and the DNA polymerase III alpha subunit
K97A
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mutant is able to undergo intermolecular cleavage, but not intramolecular self-cleavage
L101G/R102G
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mutant enzyme is defective in RecA-ssDNA-facilitated self-cleavage in vivo, can undergo RecA-ssDNA-facilitated cleavage in vitro, can interact directly with the RecA-ssDNA nucleoprotein filament in vitro, and is active in SOS mutagenesis in vivo
L40C
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less than 30% of the wild-type activity, although defective in UV mutagenesis and in vitro RecA-mediated cleavage, mutant is able to be cleaved efficiently by RecA in vivo
L44C
L9A/R10A/E11A/I12A
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heterodimer with UmuD' displays a significant increase in stability
N41D
P27S
P48G
expression of UmuD2 P48G is substantially lower than that of wild type UmuD2
Q23P/S60A
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UmuD is non-cleavable via an intramolecular cleavage pathway, but it remains cleavable via the intermolecular pathway
R37A
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when mutation is present in the UmuD' subunit of a UmuD/D' heterodimer it causes this subunit to be degraded substantially more slowly than its wild-type counterpart, when the mutation is present in the UmuD subunit of the heterodimer degradation of the UmuD' subunit occurs as efficiently as with the wild-type enzyme
S112C
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4-azidoiodoacetanilide-modified mutant, cross-links moderately efficiently with RecA
S19C
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4-azidoiodoacetanilide-modified mutant, almost no cross-linking with RecA
S57C
S60A
S60C
S67C
S81C
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4-azidoiodoacetanilide-modified mutant, cross-links most efficiently with RecA
T14A/F15A/F18A
decrease of induced mutagenesis to 20% of wild-type level, no cleavage of UmuD
V135S/K136A/R139A
expression of UmuD2 V135S/K136A/R139A is substantially lower than that of wild type UmuD2
V34C
Y33C
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less than 30% of the wild-type activity, although defective in UV mutagenesis and in vitro RecA-mediated cleavage, mutant is able to be cleaved efficiently by RecA in vivo
C24A
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site-directed mutagenesis, that removes the cleavage site Cys residue of UmuD, the mutation does not substantially affect UmuD function, cleavage site variant
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C25D
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site-directed mutagenesis, that removes the cleavage site Cys residue of UmuD, the mutation does not substantially affect UmuD function, cleavage site variant. For cleavage to occur, UmuD UmuD G25D dimer 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
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N41D
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site-directed mutagenesis, the monomeric UmuD N41D variant can only cleave in the cis conformation
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S60A
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site-directed mutagenesis, a non-cleavable mutant of UmuD and UmuD', inactive active site mutant. For cleavage to occur, UmuD S60A dimer 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
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additional information
C24A
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ability to participate in UV mutagenesis and RecA-mediated cleavage are similar to that of the wild-type enzyme
C24A
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site-directed mutagenesis, that removes the cleavage site Cys residue of UmuD, the mutation does not substantially affect UmuD function, cleavage site variant
L44C
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4-azidoiodoacetanilide-modified mutant, almost no cross-linking with RecA
N41D
the mutant generates stable, active UmuD and UmuDÂ’ monomers that functionally mimic the dimeric wild type proteins. The mutant is proficient for cleavage and interacts physically with DNA polymerase IV (DinB) and the beta-clamp, facilitates UV-induced mutagenesis and promotes overall cell viability
N41D
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site-directed mutagenesis, the monomeric UmuD N41D variant can only cleave in the cis conformation
S57C
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4-azidoiodoacetanilide-modified mutant, cross-links moderately efficiently with RecA
S60A
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site-directed mutagenesis, a non-cleavable mutant of UmuD and UmuD', inactive active site mutant. For cleavage to occur, UmuD S60A dimer 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
S60C
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similar in iodoacetate reactivity but cross-links less efficiently by I2 oxidation than the wild-type enzyme, reduced activity in UV mutagenesis
S67C
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4-azidoiodoacetanilide-modified mutant, cross-links moderately efficiently with RecA
V34C
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4-azidoiodoacetanilide-modified mutant, cross-links most efficiently with RecA
additional information
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generation of isogenic mutant UmuDC homologues A1S_0636-A1S_0637, A1S_1174-A1S_1173, and A1S_1389, the mutants are less able to acquire resistance to rifampin and streptomycin through the activities of their error-prone DNA polymerase, but neither the growth rate nor the UV-related survival of any of the three mutants is significantly different from that of the wild-type parental strain
additional information
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generation of isogenic mutant UmuDC homologues A1S_0636-A1S_0637, A1S_1174-A1S_1173, and A1S_1389, the mutants are less able to acquire resistance to rifampin and streptomycin through the activities of their error-prone DNA polymerase, but neither the growth rate nor the UV-related survival of any of the three mutants is significantly different from that of the wild-type parental strain
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additional information
characterization of two truncation variants of the Escherichia coli polymerase manager protein UmuD, UmuDELTA 8 (UmuD DELTA1-7) and UmuDELTA 18 (UmuS DELTA1-17). The loss of the N-terminal seven amino acids of UmuD results in changes in conformation of the N-terminal arms. UmuD 8 is cleaved as efficiently as full-length UmuD in vitro and in vivo, but expression of a plasmid-borne non-cleavable variant of UmuD 8 causes hypersensitivity to UV irradiation. UmuD 18 does not cleave to form UmuD', but confers resistance to UV radiation. Removal of the N-terminal seven residues of UmuD maintains its interactions with the alpha polymerase subunit of DNA polymerase III as well as its ability to disrupt interactions between alpha and the beta processivity clamp, whereas deletion of the N-terminal 17 residues results in decreases in binding to alpha and in the ability to disrupt the alpha-beta interaction. UmuD 8 mimics full-length UmuD in many respects, whereas UmuD 18 lacks a number of functions characteristic of UmuD. Deletion of the first eight residues does not change the cross-linking efficiency compared to UmuD. Deletion of the first 18 residues causes increased cross-linking efficiency, which is likely due to reduced interaction between the arms and the globular domain in the case of UmuD 18
additional information
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characterization of two truncation variants of the Escherichia coli polymerase manager protein UmuD, UmuDELTA 8 (UmuD DELTA1-7) and UmuDELTA 18 (UmuS DELTA1-17). The loss of the N-terminal seven amino acids of UmuD results in changes in conformation of the N-terminal arms. UmuD 8 is cleaved as efficiently as full-length UmuD in vitro and in vivo, but expression of a plasmid-borne non-cleavable variant of UmuD 8 causes hypersensitivity to UV irradiation. UmuD 18 does not cleave to form UmuD', but confers resistance to UV radiation. Removal of the N-terminal seven residues of UmuD maintains its interactions with the alpha polymerase subunit of DNA polymerase III as well as its ability to disrupt interactions between alpha and the beta processivity clamp, whereas deletion of the N-terminal 17 residues results in decreases in binding to alpha and in the ability to disrupt the alpha-beta interaction. UmuD 8 mimics full-length UmuD in many respects, whereas UmuD 18 lacks a number of functions characteristic of UmuD. Deletion of the first eight residues does not change the cross-linking efficiency compared to UmuD. Deletion of the first 18 residues causes increased cross-linking efficiency, which is likely due to reduced interaction between the arms and the globular domain in the case of UmuD 18
additional information
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characterization of two truncation variants of the Escherichia coli polymerase manager protein UmuD, UmuDELTA 8 (UmuD DELTA1-7) and UmuDELTA 18 (UmuS DELTA1-17). The loss of the N-terminal seven amino acids of UmuD results in changes in conformation of the N-terminal arms. UmuD 8 is cleaved as efficiently as full-length UmuD in vitro and in vivo, but expression of a plasmid-borne non-cleavable variant of UmuD 8 causes hypersensitivity to UV irradiation. UmuD 18 does not cleave to form UmuD', but confers resistance to UV radiation. Removal of the N-terminal seven residues of UmuD maintains its interactions with the alpha polymerase subunit of DNA polymerase III as well as its ability to disrupt interactions between alpha and the beta processivity clamp, whereas deletion of the N-terminal 17 residues results in decreases in binding to alpha and in the ability to disrupt the alpha-beta interaction. UmuD 8 mimics full-length UmuD in many respects, whereas UmuD 18 lacks a number of functions characteristic of UmuD. Deletion of the first eight residues does not change the cross-linking efficiency compared to UmuD. Deletion of the first 18 residues causes increased cross-linking efficiency, which is likely due to reduced interaction between the arms and the globular domain in the case of UmuD 18
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