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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
diphosphate + H2O
2 phosphate
-
low activity
-
-
?
diphosphate + H2O
phosphate + phosphate
-
low activity
-
-
?
ditrans,octacis-undecaprenyl diphosphate + H2O
ditrans,octacis-undecaprenyl phosphate + phosphate
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
isopentenyl diphosphate + H2O
isopentenyl phosphate + phosphate
phosphatidic acid + H2O
?
-
low activity
-
-
?
phosphatidylglycerol phosphate + H2O
phosphatidylglycerol + phosphate
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
additional information
?
-
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
low activity
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
low activity
-
-
?
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
-
low activity
-
-
?
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
-
low activity
-
-
?
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
-
relatively good substrate
-
-
?
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
-
-
-
-
?
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
-
-
-
?
isopentenyl diphosphate + H2O
isopentenyl phosphate + phosphate
-
low activity
-
-
?
isopentenyl diphosphate + H2O
isopentenyl phosphate + phosphate
-
low activity
-
-
?
isopentenyl diphosphate + H2O
isopentenyl phosphate + phosphate
-
-
-
-
?
isopentenyl diphosphate + H2O
isopentenyl phosphate + phosphate
-
-
-
-
?
phosphatidylglycerol phosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
-
?
phosphatidylglycerol phosphate + H2O
phosphatidylglycerol + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
involved in cyclic peptidoglycan pathway
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
low activity
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
the dephosphorylation of Und-PP, from de novo synthesis, produces undecaprenyl phosphate, a universal lipid carrier of glycan biosynthetic intermediates for carbohydrate polymers that are exported to the bacterial cell envelope, YbjG and YeiU are implicated in the recycling of periplasmic Und-PP molecules
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
the synthesis of the lipid carrier undecaprenyl phosphate, C55-P, requires the dephosphorylation of its precursor, undecaprenyl pyrophosphate, C55-PP, the dephosphorylation involves four integral membrane proteins, BacA, and three members of the type 2 phosphatidic acid phosphatase family, PgpB, YbjG, and YeiU, overview
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
involved in cyclic peptidoglycan pathway
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
?
additional information
?
-
-
undecaprenyl phosphate is no substrate, no activity on monophosphate compounds is observed. PbrB cannot dephosphorylate phosphatidic acid or glucose-6-phosphate
-
-
?
additional information
?
-
-
undecaprenyl phosphate is no substrate, no activity on monophosphate compounds is observed. PbrB cannot dephosphorylate phosphatidic acid or glucose-6-phosphate
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
no activity with isopentenyl diphosphate, phosphatidylglycerol phosphate and phosphatidic acid
-
-
-
additional information
?
-
-
no activity with phosphatidic acid
-
-
-
additional information
?
-
-
no activity with phosphatidic acid
-
-
-
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ditrans,octacis-undecaprenyl diphosphate + H2O
ditrans,octacis-undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
involved in cyclic peptidoglycan pathway
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
the dephosphorylation of Und-PP, from de novo synthesis, produces undecaprenyl phosphate, a universal lipid carrier of glycan biosynthetic intermediates for carbohydrate polymers that are exported to the bacterial cell envelope, YbjG and YeiU are implicated in the recycling of periplasmic Und-PP molecules
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
the synthesis of the lipid carrier undecaprenyl phosphate, C55-P, requires the dephosphorylation of its precursor, undecaprenyl pyrophosphate, C55-PP, the dephosphorylation involves four integral membrane proteins, BacA, and three members of the type 2 phosphatidic acid phosphatase family, PgpB, YbjG, and YeiU, overview
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
involved in cyclic peptidoglycan pathway
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
-
-
-
?
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(5-bromo-2-[[3-(octyloxy)phenyl]methoxy]phenyl)phosphonic acid
-
-
2-(N-methyl-3-(octyloxy)benzamido)phenylphosphonic acid
-
-
2-methoxy-6-[3-(octyloxy)benzamido]benzoic acid
-
-
2-[3,4-bis(2-methoxyethoxy)benzamido]-5-bromobenzoic acid
-
-
2-[3-(hexyloxy)benzamido]benzoic acid
-
-
2-[3-(octyloxy)benzamido]-5-(trifluoromethoxy)benzoic acid
-
most potent inhibitor
2-[3-(octyloxy)benzamido]-5-phosphonobenzoic acid
-
-
2-[3-(octyloxy)benzamido]benzoic acid
-
-
2-[methyl[3-(octyloxy)benzoyl]amino]benzoic acid
-
-
3,4,5-trimethoxy-2-[3-(octyloxy)benzamido]benzoic acid
-
-
3-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
3-[3-(hexyloxy)benzamido]-4-hydroxybenzoic acid
-
-
3-[3-(octyloxy)benzamido]benzene-1,2-dicarboxylic acid
-
-
3-[3-(octyloxy)benzamido]benzoic acid
-
-
4,5-difluoro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
4-hydroxy-3-[3-(octyloxy)benzamido]benzoic acid
-
-
4-[3-(octyloxy)benzamido]benzene-1,3-dicarboxylic acid
-
-
5-(diethoxyphosphoryl)-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-(methanesulfonyl)-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-bromo-2-[3-(3,3-dimethylbut-1-yn-1-yl)benzamido]benzoic acid
-
-
5-bromo-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-chloro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-fluoro-2-(3-(octyloxy)benzamido)benzoic acid
-
-
5-fluoro-2-[3-(hexyloxy)benzamido]benzoic acid
-
-
5-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-hydroxy-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-methoxy-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-methoxy-4-(2-methoxyethoxy)-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-nitro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-[3-(octyloxy)benzamido]benzene-1,3-dicarboxylic acid
-
-
Ca2+
about less than 10% residual activity at 10 mM
Cu2+
complete inhibition at 10 mM
Mn2+
about 90% residual activity at 10 mM
N-(2-carbamoylphenyl)-3-(octyloxy)benzamide
-
-
n-Propanol
-
inhibitory at concentrations above 1.5 M
p-chloromercuriphenylsulfonic acid
-
-
tetrahydrofuran
-
inhibitory at concentrations above 2 M
tripropeptin C
tripropeptin C can potentially inhibit C55-PP phosphatase activity, which plays a crucial role in the lipid cycle of peptidoglycan synthesis
Zn2+
about less than 10% residual activity at 10 mM
[2-[3-(octyloxy)benzamido]phenyl]phosphonic acid
-
-
[3-[3-(octyloxy)benzamido]phenyl]phosphonic acid
-
-
bacitracin
-
-
bacitracin
-
partial inhibition at 10 mM bacitracin
bacitracin
-
complex formation with substrate + metal ion, reversed by addition of chelating agents
EDTA
5 mM, complete loss of activity
EDTA
-
95% inhibition at 0.05 mM, 98% inhibition at 1 mM
EDTA
-
complete inhibition at 5 mM
EDTA
complete inhibition at 0.001 mM
additional information
-
no inhibitory effect by reserpine
-
additional information
-
the enzyme is not inhibited by Pb2+ (0.0001-10 mM)
-
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0.0067
(5-bromo-2-[[3-(octyloxy)phenyl]methoxy]phenyl)phosphonic acid
0.0065
2-(N-methyl-3-(octyloxy)benzamido)phenylphosphonic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.2
2-methoxy-6-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.2
2-[3,4-bis(2-methoxyethoxy)benzamido]-5-bromobenzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.045
2-[3-(hexyloxy)benzamido]benzoic acid
0.00083
2-[3-(octyloxy)benzamido]-5-(trifluoromethoxy)benzoic acid
0.0042
2-[3-(octyloxy)benzamido]-5-phosphonobenzoic acid
0.01
2-[3-(octyloxy)benzamido]benzoic acid
0.2
2-[methyl[3-(octyloxy)benzoyl]amino]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.2
3,4,5-trimethoxy-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0085
3-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.031
3-[3-(hexyloxy)benzamido]-4-hydroxybenzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.2
3-[3-(octyloxy)benzamido]benzene-1,2-dicarboxylic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.073
3-[3-(octyloxy)benzamido]benzoic acid
0.0034
4,5-difluoro-2-[3-(octyloxy)benzamido]benzoic acid
0.031
4-hydroxy-3-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.2
4-[3-(octyloxy)benzamido]benzene-1,3-dicarboxylic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0085 - 0.2
5-(diethoxyphosphoryl)-2-[3-(octyloxy)benzamido]benzoic acid
0.0098
5-(methanesulfonyl)-2-[3-(octyloxy)benzamido]benzoic acid
0.2
5-bromo-2-[3-(3,3-dimethylbut-1-yn-1-yl)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0042
5-bromo-2-[3-(octyloxy)benzamido]benzoic acid
0.003
5-chloro-2-[3-(octyloxy)benzamido]benzoic acid
0.0027
5-fluoro-2-(3-(octyloxy)benzamido)benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.02
5-fluoro-2-[3-(hexyloxy)benzamido]benzoic acid
0.0013 - 0.0027
5-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
0.011
5-hydroxy-2-[3-(octyloxy)benzamido]benzoic acid
0.2
5-methoxy-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.2
5-methoxy-4-(2-methoxyethoxy)-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0013
5-nitro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.2
5-[3-(octyloxy)benzamido]benzene-1,3-dicarboxylic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.2
N-(2-carbamoylphenyl)-3-(octyloxy)benzamide
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.00003 - 0.0001
tripropeptin C
Micrococcus luteus
in 100 mM Tris-HCl, 10 mM MgCl2 and 3.9 mM n-dodecyl-beta-maltoside (pH 7.5), 1.25 mM CaCl2, at 30°C
0.0065
[2-[3-(octyloxy)benzamido]phenyl]phosphonic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.0071
[3-[3-(octyloxy)benzamido]phenyl]phosphonic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.0067
(5-bromo-2-[[3-(octyloxy)phenyl]methoxy]phenyl)phosphonic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.0067
(5-bromo-2-[[3-(octyloxy)phenyl]methoxy]phenyl)phosphonic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.045
2-[3-(hexyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.045
2-[3-(hexyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.00083
2-[3-(octyloxy)benzamido]-5-(trifluoromethoxy)benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.00083
2-[3-(octyloxy)benzamido]-5-(trifluoromethoxy)benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.0042
2-[3-(octyloxy)benzamido]-5-phosphonobenzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.0042
2-[3-(octyloxy)benzamido]-5-phosphonobenzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.01
2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.01
2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.073
3-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.073
3-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.0034
4,5-difluoro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.0034
4,5-difluoro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.0085
5-(diethoxyphosphoryl)-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.2
5-(diethoxyphosphoryl)-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0098
5-(methanesulfonyl)-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.0098
5-(methanesulfonyl)-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.0042
5-bromo-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.0042
5-bromo-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.003
5-chloro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.003
5-chloro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.02
5-fluoro-2-[3-(hexyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.02
5-fluoro-2-[3-(hexyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.0013
5-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.0027
5-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.011
5-hydroxy-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.011
5-hydroxy-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.032
bacitracin
Escherichia coli
-
pH and temperature not specified in the publication
0.032
bacitracin
Escherichia coli
-
at pH 7.5 and 20°C
0.033
bacitracin
Escherichia coli
pH 7.0, 37°C
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malfunction
an undecaprenyl pyrophosphate phosphatase null mutant does not show any significant growth or morphological defect, neither is its sensitivity to bacitracin affected. However, the enzyme activity in the mutant is reduced by 75%
malfunction
-
enzyme deletion results in a mutant with reduced biofilm formation that is highly sensitive to bacitracin, but confers more resistance to lactococcin G
malfunction
-
enzyme depletion disrupts cell envelope biogenesis in Bacillus subtilis and leads to morphological defects consistent with a failure of cell envelope synthesis and strongly activates the sigmaM-dependent cell envelope stress response
malfunction
-
single uppP or bcrC enzyme deletions show no or less than 0.1% misshaped cells. In contrast, both enzyme depletions leads to a severe phenotype during exponential growth phase
malfunction
-
enzyme deletion results in a mutant with reduced biofilm formation that is highly sensitive to bacitracin, but confers more resistance to lactococcin G
-
physiological function
the enzyme confers resistance to bacitracin
physiological function
mutants lacking enzymic activity show no significant changes in growth rate, colony morphology and biofilm formation. The mutants exhibit increased susceptibility to bacitracin. When the enzyme is expressed in a wild-type background, the minimum inhibitory concentration of bacitracin increases to 256 mg/L. The minimum inhibitory concentrations of cefoxitin, teicoplanin, vancomycin, gentamicin, enrofloxacin and D-cycloserine are unaltered in the mutant relative to the wild-type, as are susceptibilities to other stress agents such as glycine, lysozyme, NaCl, SDS, low and high pH, oxidative stress and ethanol
physiological function
-
the enzyme BcrC is more relevant during vegetative growth while the enzyme UppP is crucial for normal sporulation. Together, enzyme forms bcrC and uppP encode the essential undecaprenyl diphosphatase function of Bacillus subtilis
physiological function
-
the enzyme is essential in vivo for stomach colonization and is also involved in cationic antimicrobial peptide resistance
physiological function
-
the enzyme plays important roles in cell wall biosynthesis and bacitracin resistance
physiological function
-
the enzyme is essential in vivo for stomach colonization and is also involved in cationic antimicrobial peptide resistance
-
physiological function
-
the enzyme plays important roles in cell wall biosynthesis and bacitracin resistance
-
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D111A
mutation in membrane-water interface, 100% residual activity
D150A
mutation in membrane-water interface, 64% residual activity
D43A
mutation in aequous interface, 73% residual activity
E17A
mutation within the consensus regions, 26% residiual activity
E17A/E21A
mutation within the consensus regions, mutant is completely inactive
E194A
mutation in aequous interface, 31% residual activity
E41A
mutation in aequous interface, 85% residual activity
E49A
mutation in membrane-water interface, 36% residual activity
Q164A
-
the mutant shows 24.3% of wild type activity
Q53A
mutation in membrane-water interface, 14% residual activity
R261A
completely inactive
S196A
-
the mutant shows 36.8% of wild type activity
S26A
-
the mutant shows 15% of wild type activity
T178A
mutation within the consensus regions, mutant is completely inactive
G163R
the mutation leads to no protein expression at all
G168A
the mutation leads to no protein expression at all
S167A
the mutant shows 34% of wild type activity
S22A
the mutant shows less than 1.3% of wild type activity
S23A
the mutant shows 65% of wild type activity
additional information
-
construction of chromosomal gene deletions mutants, double and triple deletion mutants in the genes uppP and ybjG, and uppP, ybjG and yeiU, respectively, are supersensitive to the Und-P de novo biosynthesis inhibitor fosmidomycin, while single or combined deletions including pgpB have no effect on fosmidomycin supersensitivity, overview
E21A
mutation within the consensus regions, 40% residiual activity
E21A
-
the mutant shows 1.4% of wild type activity
H30A
mutation within the consensus regions, mutant is completely inactive
H30A
-
the mutant shows 6.2% of wild type activity
R174A
mutation within the consensus regions, mutant is completely inactive
R174A
-
the mutant shows 0.13% of wild type activity
R189A
mutation in aequous interface, 11% residual activity
R189A
-
the mutant shows 12.1% of wild type activity
S173A
mutation within the consensus regions, mutant is completely inactive
S173A
-
the mutant shows 2.2% of wild type activity
S175A
-
the mutant shows 41% of wild type activity
S175A
mutation within the consensus regions, 32% residiual activity
S27A
inactive
S27A
-
the mutant shows 0.013% of wild type activity
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