BRENDA - Enzyme Database show
show all sequences of 2.7.8.43

Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation

Zhou, Z.; Ribeiro, A.A.; Lin, S.; Cotter, R.J.; Miller, S.I.; Raetz, C.R.; J. Biol. Chem. 276, 43111-43121 (2001)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of a pmrA- null mutant strain JSG421 of covalently modified pmrAc strains JSG485 and JSG486, overview
Salmonella enterica subsp. enterica serovar Typhimurium
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Salmonella enterica subsp. enterica serovar Typhimurium
the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview
?
-
-
-
additional information
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
-
gene pmrA
-
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
-
gene pmrA
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview
734138
Salmonella enterica subsp. enterica serovar Typhimurium
?
-
-
-
-
additional information
the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview
734138
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
?
-
-
-
-
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of a pmrA- null mutant strain JSG421 of covalently modified pmrAc strains JSG485 and JSG486, overview
Salmonella enterica subsp. enterica serovar Typhimurium
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Salmonella enterica subsp. enterica serovar Typhimurium
the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview
?
-
-
-
additional information
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview
734138
Salmonella enterica subsp. enterica serovar Typhimurium
?
-
-
-
-
additional information
the enzyme modifies lipid A with one or two phosphoethanolamine moieties. Six lipid A substrate subtypes, St1 to St6, from wild type Salmonella typhimurium are covalently modified with one or two 4-amino-4-deoxy-L-arabinose moieties. Each lipid A species with a defined set of polar modifications can be further derivatized with a palmitoyl moiety and/or a 2-hydroxymyristoyl residue in place of the secondary myristoyl chain at position 3', high resolution NMR spectroscopy and mass spectrometry analysis of lipid A profiles from wild-type strain 14028 and mutant strains, overview
734138
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
?
-
-
-
-
General Information
General Information
Commentary
Organism
physiological function
enzyme PmrA is required for production of lipid A species with one or two phosphoethanolamine or 4-amino-4-deoxy-L-arabinose substituents. PmrA is not needed for the incorporation of 2-hydroxymyristate or palmitate into lipid A
Salmonella enterica subsp. enterica serovar Typhimurium
General Information (protein specific)
General Information
Commentary
Organism
physiological function
enzyme PmrA is required for production of lipid A species with one or two phosphoethanolamine or 4-amino-4-deoxy-L-arabinose substituents. PmrA is not needed for the incorporation of 2-hydroxymyristate or palmitate into lipid A
Salmonella enterica subsp. enterica serovar Typhimurium
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)
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A phosphoethanolamine transfer ...
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121
1444-1456
2016
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1
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2
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735018
Trombley
Phosphoethanolamine transferas ...
Haemophilus ducreyi, Haemophilus ducreyi ATCC 700724
PLoS ONE
10
e0124373
2015
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1
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1
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7
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3
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739106
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Extracellular zinc induces pho ...
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166-178
2015
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1
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2
1
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740532
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Shewanella algae, Shewanella algae MARS 14
Int. J. Antimicrob. Agents
46
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2015
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1
1
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738368
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Phosphoethanolamine decoration ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
Infect. Immun.
82
2170-2179
2014
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1
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2
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10
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2
2
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739495
Piek
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Neisseria meningitidis, Neisseria meningitidis NMB
PLoS ONE
9
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2014
1
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1
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1
1
1
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1
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8
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1
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739786
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70
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2014
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1
1
6
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1
1
1
7
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3
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1
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12
2
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6
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7
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1
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12
2
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3
3
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733965
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Phosphoethanolamine residues o ...
Neisseria gonorrhoeae
Infect. Immun.
81
33-42
2013
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2
2
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733966
Cullen
EptC of Campylobacter jejuni m ...
Campylobacter jejuni, Campylobacter jejuni 81-176
Infect. Immun.
81
430-4440
2013
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1
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1
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3
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8
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2
2
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734476
Wanty
The structure of the neisseria ...
Neisseria meningitidis, Neisseria meningitidis NMB
J. Mol. Biol.
425
3389-3402
2013
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1
1
1
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1
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3
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1
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4
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740134
Bontemps-Gallo
Biosynthesis of osmoregulated ...
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BioMed Res. Int.
2013
371429
2013
1
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1
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1
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740516
Knirel
O-antigen structure of Shigell ...
Shigella flexneri
Glycobiology
23
475-485
2013
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733017
Anandan
Cloning, expression, purificat ...
Neisseria meningitidis, Neisseria meningitidis NMB
Acta Crystallogr. Sect. F
68
1494-1497
2012
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1
1
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734190
Cullen
Trent, M.S.: Characterization ...
Campylobacter jejuni, Campylobacter jejuni 81-176
J. Biol. Chem.
287
326-3336
2012
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734198
Farizano
The PmrAB system-inducing cond ...
Salmonella enterica 14028s, Salmonella enterica
J. Biol. Chem.
287
38778-38789
2012
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3
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733107
Beceiro
Phosphoethanolamine modificati ...
Acinetobacter baumannii
Antimicrob. Agents Chemother.
55
3370-3379
2011
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1
3
3
1
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723212
Herrera
Activation of PmrA inhibits Lp ...
Escherichia coli, Salmonella enterica, Salmonella enterica LT2
Mol. Microbiol.
76
1444-1460
2010
1
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5
2
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735157
Cullen
A link between the assembly of ...
Campylobacter jejuni
Proc. Natl. Acad. Sci. USA
107
5160-5165
2010
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1
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2
2
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733963
Lewis
Phosphoethanolamine substituti ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA19
Infect. Immun.
77
1112-1120
2009
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-
1
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1
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-
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4
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3
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6
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1
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1
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4
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6
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1
1
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733962
Takahashi
Modification of lipooligosacch ...
Neisseria meningitidis
Infect. Immun.
76
5777-5789
2008
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1
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1
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4
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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
2
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734067
Tamayo
Identification of cptA, a PmrA ...
Salmonella enterica, Salmonella enterica LT2
J. Bacteriol.
187
3391-3399
2005
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1
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4
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5
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4
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2
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4
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4
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2
4
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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.
280
28186-28194
2005
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1
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3
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1
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5
5
-
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734064
Lee
The PmrA-regulated pmrC gene m ...
Salmonella enterica
J. Bacteriol.
186
4124-4133
2004
1
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1
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1
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3
3
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734148
Tran
Periplasmic cleavage and modif ...
Helicobacter pylori
J. Biol. Chem.
279
55780-55791
2004
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1
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4
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3
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1
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3
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3
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-
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2
2
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734062
Cox
Phosphorylation of the lipid A ...
Neisseria meningitidis
J. Bacteriol.
185
3270-3277
2003
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1
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1
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1
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3
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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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-
-
-
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2
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.
276
43111-43121
2001
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1
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2
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2
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1
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2
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2
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-
-
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1
1
-
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734706
Gunn
PmrA-PmrB-regulated genes nece ...
Salmonella enterica 14028s, Salmonella enterica
Mol. Microbiol.
27
1171-1182
1998
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1
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3
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1
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2
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