BRENDA - Enzyme Database show
show all sequences of 2.7.8.43

The role of oxidoreductases in determining the function of the neisserial lipid A phosphoethanolamine transferase required for resistance to polymyxin

Piek, S.; Wang, Z.; Ganguly, J.; Lakey, A.M.; Bartley, S.N.; Mowlaboccus, S.; Anandan, A.; Stubbs, K.A.; Scanlon, M.J.; Vrielink, A.; Azadi, P.; Carlson, R.W.; Kahler, C.M.; PLoS ONE 9, e106513 (2014)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
the neisserial oxidoreductase, DsbA3, contributes to the activity of LptA
Neisseria meningitidis
Cloned(Commentary)
Commentary
Organism
gene lptA, DNA and amino acid sequence determination and analysis, genotyping in Neisseria, recombinant expression of His6-tagged enzyme in Escherichi coli strain JCB570 and in Neisseria meningitidis from low copy expression vector pCMK1001. In Escherichia coli, the stability and activity of neisserial LptA::Hisx6 is entirely dependent upon the coexpression of the EcDsbA oxidoreductase. Although expression of LptA::Hisx6 and EcDsbA in Escherichia coli results in a 32fold increase in polymyxin resistance, the proportion of lipid A headgroups substituted with PEA rises to 26%
Neisseria meningitidis
Engineering
Amino acid exchange
Commentary
Organism
additional information
neisserial LptA stability is dependent on the presence of an oxidoreductase DsbA, LptA::Hisx6 expressed in JCB571 (CKEC543), in which the chromosomal copy of dsbA has been insertionally inactivated, is not stable and is rapidly removed via proteolytic degradation
Neisseria meningitidis
General Stability
General Stability
Organism
all three neisserial oxidoreductases, including DsbA1, DsbA2 and DsbA3, contribute to resistance to polymyxin
Neisseria meningitidis
Inhibitors
Inhibitors
Commentary
Organism
Structure
polymyxin
resistance to polymyxin for the enzyme is realized by oxidoreductase DsbA
Neisseria meningitidis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
LptA is an integral membrane protein
Neisseria meningitidis
16020
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
-
Neisseria meningitidis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Neisseria meningitidis
Q7DDQ9
-
-
Neisseria meningitidis NMB
Q7DDQ9
-
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichi coli strain JCB570 and Neisseria meningitidis by nickel affinity chromatography and ultrafiltration
Neisseria meningitidis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylphosphatidylethanolamine + lipid A
-
739495
Neisseria meningitidis
diacylglycerol + lipid A (2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
739495
Neisseria meningitidis NMB
diacylglycerol + lipid A (2-aminoethyl diphosphate)
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 60000, about, sequence calculation
Neisseria meningitidis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
the neisserial oxidoreductase, DsbA3, contributes to the activity of LptA
Neisseria meningitidis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene lptA, DNA and amino acid sequence determination and analysis, genotyping in Neisseria, recombinant expression of His6-tagged enzyme in Escherichi coli strain JCB570 and in Neisseria meningitidis from low copy expression vector pCMK1001. In Escherichia coli, the stability and activity of neisserial LptA::Hisx6 is entirely dependent upon the coexpression of the EcDsbA oxidoreductase. Although expression of LptA::Hisx6 and EcDsbA in Escherichia coli results in a 32fold increase in polymyxin resistance, the proportion of lipid A headgroups substituted with PEA rises to 26%
Neisseria meningitidis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
neisserial LptA stability is dependent on the presence of an oxidoreductase DsbA, LptA::Hisx6 expressed in JCB571 (CKEC543), in which the chromosomal copy of dsbA has been insertionally inactivated, is not stable and is rapidly removed via proteolytic degradation
Neisseria meningitidis
General Stability (protein specific)
General Stability
Organism
all three neisserial oxidoreductases, including DsbA1, DsbA2 and DsbA3, contribute to resistance to polymyxin
Neisseria meningitidis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
polymyxin
resistance to polymyxin for the enzyme is realized by oxidoreductase DsbA
Neisseria meningitidis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
LptA is an integral membrane protein
Neisseria meningitidis
16020
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
-
Neisseria meningitidis
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichi coli strain JCB570 and Neisseria meningitidis by nickel affinity chromatography and ultrafiltration
Neisseria meningitidis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylphosphatidylethanolamine + lipid A
-
739495
Neisseria meningitidis
diacylglycerol + lipid A (2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
739495
Neisseria meningitidis NMB
diacylglycerol + lipid A (2-aminoethyl diphosphate)
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 60000, about, sequence calculation
Neisseria meningitidis
Other publictions for EC 2.7.8.43
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
750867
Hicks
-
Structural basis for the lipo ...
Escherichia coli
Int. J. Mol. Sci.
19
E2680
2018
-
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1
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1
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1
1
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-
-
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1
1
-
-
-
752134
Schultz
Lipopolysaccharide binding to ...
Escherichia coli
Protein Sci.
26
1517-1523
2017
-
-
1
-
14
-
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1
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1
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1
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1
1
1
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1
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14
-
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1
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-
-
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1
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-
1
1
1
-
-
-
-
-
-
-
-
3
3
-
-
-
738476
Liu
A phosphoethanolamine transfer ...
Cronobacter sakazakii, Cronobacter sakazakii BAA894
J. Appl. Microbiol.
121
1444-1456
2016
-
-
1
-
1
-
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2
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4
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2
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2
2
-
-
-
733635
Handing
The lipooligosaccharide-modify ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
Cell. Microbiol.
17
910-921
2015
-
-
1
-
1
-
-
-
-
-
-
2
-
4
-
-
-
-
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2
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2
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2
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2
2
-
-
-
735018
Trombley
Phosphoethanolamine transferas ...
Haemophilus ducreyi, Haemophilus ducreyi ATCC 700724
PLoS ONE
10
e0124373
2015
-
-
1
-
1
-
-
-
-
-
-
1
-
7
-
-
-
-
-
-
-
-
5
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2
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1
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1
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-
5
-
-
-
-
-
-
-
-
-
-
2
3
-
-
-
739106
Nowicki
Extracellular zinc induces pho ...
Pseudomonas aeruginosa
Mol. Microbiol.
97
166-178
2015
-
-
1
-
1
-
-
-
-
1
-
1
-
4
-
-
-
-
-
-
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2
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1
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1
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1
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1
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2
-
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-
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-
-
1
2
2
1
-
-
740532
Telke
Functional genomics to discove ...
Shewanella algae, Shewanella algae MARS 14
Int. J. Antimicrob. Agents
46
648-652
2015
-
-
1
-
-
-
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2
-
2
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4
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1
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2
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4
-
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-
-
-
-
-
1
1
-
-
-
738368
Packiam
Phosphoethanolamine decoration ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
Infect. Immun.
82
2170-2179
2014
-
-
-
-
1
-
-
-
-
-
-
2
-
11
-
-
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-
-
-
-
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2
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1
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2
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-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
739495
Piek
The role of oxidoreductases in ...
Neisseria meningitidis, Neisseria meningitidis NMB
PLoS ONE
9
e106513
2014
1
-
1
-
1
1
1
-
1
-
1
-
-
8
-
-
1
-
-
-
-
-
2
1
-
-
-
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-
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1
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1
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1
1
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1
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1
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1
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1
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-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
739786
Fage
Crystallographic study of the ...
Campylobacter jejuni, Campylobacter jejuni 81-176
Acta Crystallogr. Sect. D
70
2730-2739
2014
-
-
1
1
6
-
-
-
1
1
1
7
-
3
-
1
1
-
-
-
-
-
12
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
6
-
-
-
-
-
1
1
1
7
-
-
1
1
-
-
-
-
12
2
-
-
-
-
-
-
-
-
-
3
3
-
-
-
752031
Sherman
Decoupling catalytic activity ...
Neisseria meningitidis serogroup B, Neisseria meningitidis serogroup B MC58
Proc. Natl. Acad. Sci. USA
111
4982-4987
2014
-
-
-
-
-
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-
-
1
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2
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1
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-
-
-
-
-
-
-
2
2
-
-
-
733965
Lewis
Phosphoethanolamine residues o ...
Neisseria gonorrhoeae
Infect. Immun.
81
33-42
2013
-
-
-
-
-
-
-
-
-
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1
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-
-
-
-
-
-
-
2
2
-
-
-
733966
Cullen
EptC of Campylobacter jejuni m ...
Campylobacter jejuni, Campylobacter jejuni 81-176
Infect. Immun.
81
430-4440
2013
-
-
1
-
1
-
-
-
-
-
-
8
-
3
-
-
-
-
-
-
-
-
8
-
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-
-
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-
-
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1
-
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1
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8
-
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-
-
8
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
734476
Wanty
The structure of the neisseria ...
Neisseria meningitidis, Neisseria meningitidis NMB
J. Mol. Biol.
425
3389-3402
2013
-
-
1
1
1
-
1
-
-
3
-
6
-
8
-
1
1
-
-
-
-
-
12
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
1
1
-
-
1
-
-
-
5
-
6
-
-
1
1
-
-
-
-
12
1
-
-
-
-
-
-
-
-
-
3
4
-
-
-
740134
Bontemps-Gallo
Biosynthesis of osmoregulated ...
Escherichia coli
BioMed Res. Int.
2013
371429
2013
1
-
1
-
1
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-
-
1
-
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1
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3
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2
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1
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1
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2
-
1
-
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-
-
-
-
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1
1
-
-
-
740516
Knirel
O-antigen structure of Shigell ...
Shigella flexneri
Glycobiology
23
475-485
2013
-
-
1
-
-
-
-
-
-
-
-
3
-
4
-
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5
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1
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3
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-
-
5
-
-
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-
-
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-
1
1
-
-
-
733017
Anandan
Cloning, expression, purificat ...
Neisseria meningitidis, Neisseria meningitidis NMB
Acta Crystallogr. Sect. F
68
1494-1497
2012
-
-
1
1
1
-
-
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1
-
-
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7
-
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1
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-
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1
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1
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1
1
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1
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1
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1
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1
1
-
-
-
734190
Cullen
Trent, M.S.: Characterization ...
Campylobacter jejuni, Campylobacter jejuni 81-176
J. Biol. Chem.
287
326-3336
2012
-
-
-
-
-
-
-
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-
6
-
8
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8
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6
-
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8
-
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-
-
-
-
-
-
-
2
2
-
-
-
734198
Farizano
The PmrAB system-inducing cond ...
Salmonella enterica 14028s, Salmonella enterica
J. Biol. Chem.
287
38778-38789
2012
-
-
-
-
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-
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3
-
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-
-
-
-
-
-
3
3
-
-
-
733107
Beceiro
Phosphoethanolamine modificati ...
Acinetobacter baumannii
Antimicrob. Agents Chemother.
55
3370-3379
2011
-
-
1
-
-
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1
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1
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1
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1
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1
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1
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-
-
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-
-
1
3
3
1
-
-
723212
Herrera
Activation of PmrA inhibits Lp ...
Escherichia coli, Salmonella enterica, Salmonella enterica LT2
Mol. Microbiol.
76
1444-1460
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735157
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A link between the assembly of ...
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2010
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733963
Lewis
Phosphoethanolamine substituti ...
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2009
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733962
Takahashi
Modification of lipooligosacch ...
Neisseria meningitidis
Infect. Immun.
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2008
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Identification of cptA, a PmrA ...
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2005
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734151
Tran
Resistance to the antimicrobia ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium C5
J. Biol. Chem.
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2005
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734064
Lee
The PmrA-regulated pmrC gene m ...
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J. Bacteriol.
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2004
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734148
Tran
Periplasmic cleavage and modif ...
Helicobacter pylori
J. Biol. Chem.
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2004
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734062
Cox
Phosphorylation of the lipid A ...
Neisseria meningitidis
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2003
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2
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734138
Zhou
Lipid A modifications in polym ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
J. Biol. Chem.
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2001
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734706
Gunn
PmrA-PmrB-regulated genes nece ...
Salmonella enterica 14028s, Salmonella enterica
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1998
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