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1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dihexanoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
low activity, addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dihexanoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
low activity, addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + monoolein
1,2-dioleoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + monoolein
1,2-dipalmitoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine
1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycero-3-phosphoethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
diacylphosphatidylethanolamine + arbutin
diacylglycerol + ?
arbutin is a substrate for the phosphoethanolamine transferase
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
diacylphosphatidylethanolamine + lipid A
?
a phosphoethanolamine unit is directly linked to the 1-position of the disaccharide backbone of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
diacylphosphatidylethanolamine + O-antigen serotype 4av
diacylglycerol + O-antigen serotype 4av (2-aminoethyl diphosphate)
-
the serotype 4av O-antigen has the phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor)
-
?
diacylphosphatidylethanolamine + O-antigen serotype Xv
diacylglycerol + O-antigen serotype Xv (2-aminoethyl diphosphate)
diacylphosphatidylethanolamine + O-antigen serotype Yv
diacylglycerol + O-antigen serotype Yv 3-(2-aminoethyl diphosphate)
-
the serotype Yv O-antigen has the same basic carbohydrate backbone structure as that of the classical serotype Y, but differs in the presence of phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor)
-
?
additional information
?
-
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + monoolein
1,2-dioleoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + monoolein
1,2-dioleoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + monoolein
1,2-dipalmitoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine
-
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + monoolein
1,2-dipalmitoyl-sn-glycerol + 2-oleoyl-sn-glycero-1-phosphoethanolamine
-
-
-
?
1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycero-3-phosphoethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
-
-
-
?
1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycero-3-phosphoethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
1-acyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
-
-
-
?
diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
-
-
-
-
?
diacylphosphatidylethanolamine + alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-alpha-D-Kdo-(2->4)-alpha-D-Kdo-(2->6)-lipid A
-
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
-
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
FlgG is modified at a single site Thr75, EptC is unable to modify other amino acids (e.g. serine and tyrosine), mass spectroscopic analysis, overview
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
usage of recombinant C-terminally His6-tagged substrate protein
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
A0A3Z8TVG8
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto Thr75 of FlgG proteins
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
FlgG is modified at a single site Thr75, EptC is unable to modify other amino acids (e.g. serine and tyrosine), mass spectroscopic analysis, overview
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
A0A3Z8TVG8
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto Thr75 of FlgG proteins
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
A0A3Z8TVG8
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
A0A3Z8TVG8
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
A0A3Z8TVG8
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
the phosphoethanolamine transferase is specific for the 4'-phosphate residue of Cronobacter sakazakii lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
the phosphoethanolamine transferase is specific for the 4'-phosphate residue of Cronobacter sakazakii lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
Pseudomonas aeruginosa lipid A, enzyme EptAPa-dependent addition of pEtN to the 4' phosphate group of BN2 and PA14 lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + O-antigen serotype Xv
diacylglycerol + O-antigen serotype Xv (2-aminoethyl diphosphate)
-
the serotype Xv O-antigen has the phosphoethanolamine on RhaII, in serotype Yv, mono- and bisphosphorylated O-units generate a block-copolymeric structure, the former being partially O-acetylated at position 6 of GlcNAc and the latter lacking O-acetylation. The serotype Xv O-antigen has the phosphoethanolamine on RhaII
-
?
diacylphosphatidylethanolamine + O-antigen serotype Xv
diacylglycerol + O-antigen serotype Xv (2-aminoethyl diphosphate)
-
-
in serotype Yv, mono- and bisphosphorylated O-units generate a block-copolymeric structure, the former being partially O-acetylated at position 6 of GlcNAc and the latter lacking O-acetylation. The serotype Xv O-antigen has the phosphoethanolamine on RhaII
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?
additional information
?
-
addition of phosphoethanolamine to hepta-acylated lipid A
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?
additional information
?
-
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
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?
additional information
?
-
the lipid A of Campylobacter jejuni is characterized by longer secondary acyl chains attached to the 2' and 3' positions of the molecule and by the addition of phosphoethanolamine to the phosphate groups attached at the 1 and 4' positions of the disaccharide backbone. The disaccharide backbone of Campylobacter jejuni lipid A is not composed solely of glucosamine residues, but can be replaced with the analogue 2,3-diamino-2,3-dideoxy-D-glucopyranose
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-
?
additional information
?
-
-
the lipid A of Campylobacter jejuni is characterized by longer secondary acyl chains attached to the 2' and 3' positions of the molecule and by the addition of phosphoethanolamine to the phosphate groups attached at the 1 and 4' positions of the disaccharide backbone. The disaccharide backbone of Campylobacter jejuni lipid A is not composed solely of glucosamine residues, but can be replaced with the analogue 2,3-diamino-2,3-dideoxy-D-glucopyranose
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?
additional information
?
-
A0A3Z8TVG8
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
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?
additional information
?
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-
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
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?
additional information
?
-
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
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?
additional information
?
-
A0A3Z8TVG8
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
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?
additional information
?
-
enzyme EptA or PmrC catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin
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?
additional information
?
-
the phosphoethanolamine cycle, overview
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-
?
additional information
?
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-
the phosphoethanolamine cycle, overview
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-
?
additional information
?
-
quantitative analysis of binding of LPS by LptA, 1:1 ratio for the LPS:LptA complex, and structure analysis of the LPS binding pocket. The entire LptA protein is affected by LPS binding, the N-terminus unfolds in the presence of LPS
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?
additional information
?
-
specific LPS interactions with LptA and LptC
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?
additional information
?
-
transfer may occur both to the 4'- and 1-phospho groups of lipid A
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-
additional information
?
-
lipid A of Helicobacter pylori lacks a 4'-phosphate group and is tri- or tetra-acylated with either (R)-3-hydroxystearate (C18) or (R)-3-hydroxypalmitate (C16), the C-1 hydroxyl group of the proximal glucosamine is derivatized with a phosphoethanolamine residue. This is in contrast with the phoshoethanolamine units of Escherichia coli, Salmonella typhimurium, and Neisseria meningitidis, which are attached to the lipid A phosphate group to form a pyrophosphate linkage. A minor lipid A species found in Helicobacter pylori is both bisphosphorylated and hexa-acylated resembling enterobacterial lipid As
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?
additional information
?
-
-
lipid A of Helicobacter pylori lacks a 4'-phosphate group and is tri- or tetra-acylated with either (R)-3-hydroxystearate (C18) or (R)-3-hydroxypalmitate (C16), the C-1 hydroxyl group of the proximal glucosamine is derivatized with a phosphoethanolamine residue. This is in contrast with the phoshoethanolamine units of Escherichia coli, Salmonella typhimurium, and Neisseria meningitidis, which are attached to the lipid A phosphate group to form a pyrophosphate linkage. A minor lipid A species found in Helicobacter pylori is both bisphosphorylated and hexa-acylated resembling enterobacterial lipid As
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?
additional information
?
-
-
phosphoethanolamine substitution at both the 1 and 4' positions of lipid A, component of lipooligosaccharide. Lipooligosaccharide structure analysis by MALDI-TOF mass spectrometry, overview
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-
?
additional information
?
-
-
phosphoethanolamine substitution at both the 1 and 4' positions of lipid A, component of lipooligosaccharide. Lipooligosaccharide structure analysis by MALDI-TOF mass spectrometry, overview
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-
?
additional information
?
-
in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
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?
additional information
?
-
-
in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
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?
additional information
?
-
in Neisseria meningitidis, phosphatidylethanolamine typically has acyl chains of C12 and C14 with the first position being occupied with a saturated chain and the second being unsaturated. The recombinant soluble periplasmic domain of the enzyme is active in an aqueous assay but unable to add phoshoethanolamine to lipid A in Escherichia coli strains, lipid A profiles, overview
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?
additional information
?
-
in Neisseria meningitidis, phosphatidylethanolamine typically has acyl chains of C12 and C14 with the first position being occupied with a saturated chain and the second being unsaturated. The recombinant soluble periplasmic domain of the enzyme is active in an aqueous assay but unable to add phoshoethanolamine to lipid A in Escherichia coli strains, lipid A profiles, overview
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-
?
additional information
?
-
-
in Neisseria meningitidis, phosphatidylethanolamine typically has acyl chains of C12 and C14 with the first position being occupied with a saturated chain and the second being unsaturated. The recombinant soluble periplasmic domain of the enzyme is active in an aqueous assay but unable to add phoshoethanolamine to lipid A in Escherichia coli strains, lipid A profiles, overview
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?
additional information
?
-
enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate
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?
additional information
?
-
enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate
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?
additional information
?
-
-
enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate
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?
additional information
?
-
enzyme activity assays on the membrane-deleted LptA are performed using 4-nitrophenyl phosphoethanolamine, p-NPPE, as the substrate analogue, the enzyme is capable of cleaving the phosphoethanolamine portion from the p-NPPE chromogenic substrate
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?
additional information
?
-
enzyme EptA catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin
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-
?
additional information
?
-
enzyme EptA catalyses the periplasmic addition of the positively charged substituent phosphoethanolamine to lipid A controlled by the PmrA transcriptional regulator and conferring resistance to cationic antimicrobial peptides, including polymyxin
-
-
?
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
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?
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
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?
additional information
?
-
lipid A substrate and product analysis by MALDI-TOF/MS. The lipidA preparations from transgenic Escherichia coli strains carrying EptA show additional ions due to the addition of phosphoethanolamine to the bis-phosphorylatedstructure and the hepta-acylated structure
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?
additional information
?
-
lipid A substrate and product analysis by MALDI-TOF/MS. The lipidA preparations from transgenic Escherichia coli strains carrying EptA show additional ions due to the addition of phosphoethanolamine to the bis-phosphorylatedstructure and the hepta-acylated structure
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additional information
?
-
NMR spectroscopic analysis of O-antigen substrates and products, detailed overview
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additional information
?
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-
NMR spectroscopic analysis of O-antigen substrates and products, detailed overview
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?
additional information
?
-
-
enzyme LptA modifies lipid A with phosphoethanolamine, mass spectrometric analysis. Haemophilus ducreyi lipopolysaccharide contains one phosphoethanolamine on its lipid A and one phosphoethanolamine on its core oligosaccharide
-
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?
additional information
?
-
enzyme LptA modifies lipid A with phosphoethanolamine, mass spectrometric analysis. Haemophilus ducreyi lipopolysaccharide contains one phosphoethanolamine on its lipid A and one phosphoethanolamine on its core oligosaccharide
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?
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1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 1-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine + lipid A
1,2-dipalmitoyl-sn-glycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
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-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
diacylphosphatidylethanolamine + lipid A
?
a phosphoethanolamine unit is directly linked to the 1-position of the disaccharide backbone of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
diacylphosphatidylethanolamine + O-antigen serotype 4av
diacylglycerol + O-antigen serotype 4av (2-aminoethyl diphosphate)
-
the serotype 4av O-antigen has the phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor)
-
?
diacylphosphatidylethanolamine + O-antigen serotype Xv
diacylglycerol + O-antigen serotype Xv (2-aminoethyl diphosphate)
-
the serotype Xv O-antigen has the phosphoethanolamine on RhaII
-
?
diacylphosphatidylethanolamine + O-antigen serotype Yv
diacylglycerol + O-antigen serotype Yv 3-(2-aminoethyl diphosphate)
-
the serotype Yv O-antigen has the same basic carbohydrate backbone structure as that of the classical serotype Y, but differs in the presence of phosphoethanolamine at position 3 of RhaIII (major) or both RhaII and RhaIII (minor)
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?
additional information
?
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diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
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diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
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?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
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-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
A0A3Z8TVG8
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-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
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-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A (2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
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-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 1-position of lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
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-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
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-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
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-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
the phosphoethanolamine transferase is specific for the 4'-phosphate residue of Cronobacter sakazakii lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
the phosphoethanolamine transferase is specific for the 4'-phosphate residue of Cronobacter sakazakii lipid A
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?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
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-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
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-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
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-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
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-
-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
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-
?
diacylphosphatidylethanolamine + lipid A
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
addition of phosphoethanolamine to the phosphate group at the 4'-position of lipid A
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?
additional information
?
-
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
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additional information
?
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the lipid A of Campylobacter jejuni is characterized by longer secondary acyl chains attached to the 2' and 3' positions of the molecule and by the addition of phosphoethanolamine to the phosphate groups attached at the 1 and 4' positions of the disaccharide backbone. The disaccharide backbone of Campylobacter jejuni lipid A is not composed solely of glucosamine residues, but can be replaced with the analogue 2,3-diamino-2,3-dideoxy-D-glucopyranose
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additional information
?
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the lipid A of Campylobacter jejuni is characterized by longer secondary acyl chains attached to the 2' and 3' positions of the molecule and by the addition of phosphoethanolamine to the phosphate groups attached at the 1 and 4' positions of the disaccharide backbone. The disaccharide backbone of Campylobacter jejuni lipid A is not composed solely of glucosamine residues, but can be replaced with the analogue 2,3-diamino-2,3-dideoxy-D-glucopyranose
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additional information
?
-
A0A3Z8TVG8
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
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?
additional information
?
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pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
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?
additional information
?
-
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
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?
additional information
?
-
A0A3Z8TVG8
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
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additional information
?
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the phosphoethanolamine cycle, overview
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additional information
?
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the phosphoethanolamine cycle, overview
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?
additional information
?
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lipid A of Helicobacter pylori lacks a 4'-phosphate group and is tri- or tetra-acylated with either (R)-3-hydroxystearate (C18) or (R)-3-hydroxypalmitate (C16), the C-1 hydroxyl group of the proximal glucosamine is derivatized with a phosphoethanolamine residue. This is in contrast with the phoshoethanolamine units of Escherichia coli, Salmonella typhimurium, and Neisseria meningitidis, which are attached to the lipid A phosphate group to form a pyrophosphate linkage. A minor lipid A species found in Helicobacter pylori is both bisphosphorylated and hexa-acylated resembling enterobacterial lipid As
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additional information
?
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lipid A of Helicobacter pylori lacks a 4'-phosphate group and is tri- or tetra-acylated with either (R)-3-hydroxystearate (C18) or (R)-3-hydroxypalmitate (C16), the C-1 hydroxyl group of the proximal glucosamine is derivatized with a phosphoethanolamine residue. This is in contrast with the phoshoethanolamine units of Escherichia coli, Salmonella typhimurium, and Neisseria meningitidis, which are attached to the lipid A phosphate group to form a pyrophosphate linkage. A minor lipid A species found in Helicobacter pylori is both bisphosphorylated and hexa-acylated resembling enterobacterial lipid As
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additional information
?
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in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
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additional information
?
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in all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
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additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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enzyme LptA modifies lipid A with phosphoethanolamine, mass spectrometric analysis. Haemophilus ducreyi lipopolysaccharide contains one phosphoethanolamine on its lipid A and one phosphoethanolamine on its core oligosaccharide
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?
additional information
?
-
enzyme LptA modifies lipid A with phosphoethanolamine, mass spectrometric analysis. Haemophilus ducreyi lipopolysaccharide contains one phosphoethanolamine on its lipid A and one phosphoethanolamine on its core oligosaccharide
-
-
?
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evolution
ethanolamine transferases are members of the YhjW/YjdB/YijP superfamily
evolution
A0A3Z8TVG8
the eptC gene (locus tag Cj0256) is clustered in a family of inner-membrane metalloenzymes (COG2194) containing a fivehelix transmembrane domain and a periplasmic catalytic domain that is currently grouped in the sulfatase family
evolution
LptA is a member of the lipopolysaccharide transport protein (Lpt) family
evolution
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the eptC gene (locus tag Cj0256) is clustered in a family of inner-membrane metalloenzymes (COG2194) containing a fivehelix transmembrane domain and a periplasmic catalytic domain that is currently grouped in the sulfatase family
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malfunction
a pbgP/pmrC double mutant resembled a pmrA mutant both in its lipid A profile and in its susceptibility to polymyxin B, mutation of the pmrC gene results in lipid A that lacks phosphoethanolamine. The inactivation of both the pmrC and pbgP genes in the polymyxin B-resistant pmrA505 genetic background reduces polymyxin B resistance to the levels of the pmrA null mutant
malfunction
although Salmonella lipid A is more prevalently modified with L-4-aminoarabinose, loss of Salmonella lpxT greatly increases modification of lipid A through enzyme EptA, and LpxT-dependent lipid A modification is not restored in the DELTAeptA mutant. LpxT catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface
malfunction
deletion of gene cj0256 results in the loss of phosphoethanolamine modification of lipid A and sensitivity to CAMPs, polymyxin B. Cj0256 mutants show decreased motility and greatly reduced flagella production. Interruption of cj0256 results in the absence of pEtN modifications on lipid A as well as FlgG. The cj0256 mutant showed a 20fold increase in sensitivity to the cationic antimicrobial peptide, polymyxin B, as well as a decrease in motility
malfunction
disruption of gene lptA leads to a approximately 10fold decrease in Neisseria meningitidis adhesion to four kinds of human endothelial and epithelial cell lines. Complementation with the lptA gene in the DELTAlptA mutant restores wild-type adherence
malfunction
eptA mutants show a 20fold decrease in polymyxin B resistanc. Overexpression of LpxT in trans in Escherichia coli strain WD101 results in loss of phosphoethanolamine modification and compromised WD101 polymyxin resistance
malfunction
-
in N-minimal media under Mg2+-limiting conditions to activate the PhoP/PhoQ two-component regulatory system, Salmonella typhimurium PhoP induces activation of PmrA, leading to increased substitution of lipid A phosphate groups with L-4-aminoarabinose and phosphoethanolamine. The mutant strain produces a lipopolysaccharide with an approximate 10fold decrease in the amount of myristate. The lipid myristoylation has an effect on the polymyxin resistance
malfunction
in three enzyme mutant strains, no phosphoethanolamine residues are included in the lipid A region of the lipopolysacchride and there is no further phosphorylation of lipid A beyond one additional phosphate species
malfunction
JSG435 carries a mutant pmrA locus allele (pmrA505) that results in high level polymyxin resistance, probably due to constitutive expression of PmrA/PmrB-activated genes
malfunction
-
loss of phosphoethanolamine from lipid A diminishes binding of the complement regulatory protein C4b binding protein (C4BP) to the FA19 porin B (PorB), providing a molecular basis to explain the susceptibility of an lptA null strain of FA19 to killing by normal human serum. Loss of phosphoethanolamine from lipid A also affects binding of the alternative pathway regulator factor H to PorB of some strains, e.g. strains 252 and 1291, but not of strains FA1090 and 273. Complementation of lptA null strains with lptA restores C4BP binding, decreased C4b deposition, and increased resistance to killing by normal human serum
malfunction
-
loss of phosphoethanolamine substitution from the lipid A component of lipooligosaccharide, due to insertional inactivation of lptA, results in increased gonococcal susceptibility to polymyxin B. Loss of phosphoethanolamine attached to lipid A at 4' position renders strain FA19 susceptible to complement killing. Serum killing of the lptA mutant occurs through the classical complement pathway. Both serum and polymyxin B resistance as well as phosphoethanolamine decoration of lipid A are restored in the lptA-null mutant by complementation with wild-type lptA
malfunction
loss of the enzyme activity increases bacterial sensitivity to killing by human complement and cationic antimicrobial peptides, lptA mutant Neisseria gonorrhoeae is significantly more sensitive to killing by human neutrophils
malfunction
phenotypes of mutants of PmrA-dependent genes pbgE2 and pbgE3, overview
malfunction
point mutations in the PmrA/B two-component system lead to colistin resistance
malfunction
strains lacking gene eptC show decreased commensal colonization of chick ceca and reduced colonization of BALB/cByJ mice compared to wild-type strains
malfunction
the eptC-deficient Campylobacter jejuni strain shows a dramatic decrease in resistance to polymyxin B when compared with wild-type, indicating a loss of phosphoethanolamine modification of the lipid A backbone. Campylobacter strains expressing site-directed FlgG mutants show defects in motility arise directly from the loss of phophoethanolamine modification of FlgG, phenotypes, overview
malfunction
-
WD101, a polymyxin-resistant Escherichia coli K-12 strain, contains a mutation in the pmrA (basR) gene resulting in a pmrAC phenotype promoting polymyxin resistance
malfunction
deletion of colR and of eptA results in loss of Zn2+-induced phosphatidylethanolamine modification of Pseudomonas aeruginosa lipid A. colR deletion mutant complementation restores Zn2+-dependent eptAPa transcription by more than fourfold
malfunction
lipid A modification is observed in strain BAA894 when the 1-phosphate residue of lipid A is removed, but disappears when the 4'-phosphate residue of lipid A was removed. When gene ESA_RS16430, the orthologous gene of Escherichia coli pmrA, is deleted in Cronobacter sakazakii strain BAA894, this phosphoethanolamine modification of lipid A is still observed, suggesting that this modification is not regulated by the PmrA-PmrB system. Compared to the wild-type strain BAA894, the ESA_RS09200 deletion mutant shows decreased resistance to cationic antimicrobial peptides, increased recognition by TLR4/MD2, and decreased ability to invade and persist in mammalian cells. Phosphoethanolamine modification of lipid A reduces recognition and killing by the host innate immune system. Analysis of mammalian cell invasion abilities of mutants using human enterocyte-like epithelial Caco-2 cells, overview
malfunction
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wild-type Neisseria gonorrhoeae strain FA1090 has a survival advantage relative to a PEA transferase A (lptA) mutant in the human urethral-challenge and murine lower genital tract infection models. Purified lipooligosaccharide containing lipid A devoid of the phosphoethanolamine modification and an lptA mutant of strain FA19 induce significantly lower levels of NF-kappaB in human embryonic kidney Toll-like receptor 4 (TLR4) cells and murine embryonic fibroblasts than wild-type lipooligosaccharide of the parent strain. Vaginal proinflammatory cytokines and chemokines are not elevated in female mice infected with the isogenic lptA mutant, in contrast to mice infected with the wild-type and complemented lptA mutant bacteria. lptA mutant bacteria are more susceptible to human and murine cathelicidins due to increased binding by these peptides and that the differential induction of NF-kappaB by wild-type and unmodified lipid A is more pronounced in the presence of cationic antimicrobial peptides. Wild-type but not lptA mutant gonococci induce a proinflammatory response during infection
malfunction
deletion of two putative PEA transferase genes in Haemophilus ducreyi increases susceptibility to HBD-3
malfunction
a mutant LptA protein unable to form oligomers has an altered affinity for LPS
malfunction
the phenotypes of Neisseria meningitidis strains lacking LptB, LptC, LptH (homologue of Escherichia coli LptA), LptF, and LptG are identical to those lacking LptD or MsbA, i.e. the knockout mutants are viable but leaky and produce only very little LPS, which is not present at the cell surface
malfunction
-
loss of phosphoethanolamine substitution from the lipid A component of lipooligosaccharide, due to insertional inactivation of lptA, results in increased gonococcal susceptibility to polymyxin B. Loss of phosphoethanolamine attached to lipid A at 4' position renders strain FA19 susceptible to complement killing. Serum killing of the lptA mutant occurs through the classical complement pathway. Both serum and polymyxin B resistance as well as phosphoethanolamine decoration of lipid A are restored in the lptA-null mutant by complementation with wild-type lptA
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malfunction
-
although Salmonella lipid A is more prevalently modified with L-4-aminoarabinose, loss of Salmonella lpxT greatly increases modification of lipid A through enzyme EptA, and LpxT-dependent lipid A modification is not restored in the DELTAeptA mutant. LpxT catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface
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malfunction
-
lipid A modification is observed in strain BAA894 when the 1-phosphate residue of lipid A is removed, but disappears when the 4'-phosphate residue of lipid A was removed. When gene ESA_RS16430, the orthologous gene of Escherichia coli pmrA, is deleted in Cronobacter sakazakii strain BAA894, this phosphoethanolamine modification of lipid A is still observed, suggesting that this modification is not regulated by the PmrA-PmrB system. Compared to the wild-type strain BAA894, the ESA_RS09200 deletion mutant shows decreased resistance to cationic antimicrobial peptides, increased recognition by TLR4/MD2, and decreased ability to invade and persist in mammalian cells. Phosphoethanolamine modification of lipid A reduces recognition and killing by the host innate immune system. Analysis of mammalian cell invasion abilities of mutants using human enterocyte-like epithelial Caco-2 cells, overview
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malfunction
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the phenotypes of Neisseria meningitidis strains lacking LptB, LptC, LptH (homologue of Escherichia coli LptA), LptF, and LptG are identical to those lacking LptD or MsbA, i.e. the knockout mutants are viable but leaky and produce only very little LPS, which is not present at the cell surface
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malfunction
-
wild-type Neisseria gonorrhoeae strain FA1090 has a survival advantage relative to a PEA transferase A (lptA) mutant in the human urethral-challenge and murine lower genital tract infection models. Purified lipooligosaccharide containing lipid A devoid of the phosphoethanolamine modification and an lptA mutant of strain FA19 induce significantly lower levels of NF-kappaB in human embryonic kidney Toll-like receptor 4 (TLR4) cells and murine embryonic fibroblasts than wild-type lipooligosaccharide of the parent strain. Vaginal proinflammatory cytokines and chemokines are not elevated in female mice infected with the isogenic lptA mutant, in contrast to mice infected with the wild-type and complemented lptA mutant bacteria. lptA mutant bacteria are more susceptible to human and murine cathelicidins due to increased binding by these peptides and that the differential induction of NF-kappaB by wild-type and unmodified lipid A is more pronounced in the presence of cationic antimicrobial peptides. Wild-type but not lptA mutant gonococci induce a proinflammatory response during infection
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malfunction
-
loss of the enzyme activity increases bacterial sensitivity to killing by human complement and cationic antimicrobial peptides, lptA mutant Neisseria gonorrhoeae is significantly more sensitive to killing by human neutrophils
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malfunction
-
in N-minimal media under Mg2+-limiting conditions to activate the PhoP/PhoQ two-component regulatory system, Salmonella typhimurium PhoP induces activation of PmrA, leading to increased substitution of lipid A phosphate groups with L-4-aminoarabinose and phosphoethanolamine. The mutant strain produces a lipopolysaccharide with an approximate 10fold decrease in the amount of myristate. The lipid myristoylation has an effect on the polymyxin resistance
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malfunction
-
strains lacking gene eptC show decreased commensal colonization of chick ceca and reduced colonization of BALB/cByJ mice compared to wild-type strains
-
malfunction
-
the eptC-deficient Campylobacter jejuni strain shows a dramatic decrease in resistance to polymyxin B when compared with wild-type, indicating a loss of phosphoethanolamine modification of the lipid A backbone. Campylobacter strains expressing site-directed FlgG mutants show defects in motility arise directly from the loss of phophoethanolamine modification of FlgG, phenotypes, overview
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malfunction
-
deletion of two putative PEA transferase genes in Haemophilus ducreyi increases susceptibility to HBD-3
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malfunction
-
phenotypes of mutants of PmrA-dependent genes pbgE2 and pbgE3, overview
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malfunction
-
JSG435 carries a mutant pmrA locus allele (pmrA505) that results in high level polymyxin resistance, probably due to constitutive expression of PmrA/PmrB-activated genes
-
metabolism
Hp0021 is the structural gene for the lipid A 1-phosphatase and is required for removal of the 1-phosphate group from mature lipid A in an in vitro assay system
metabolism
PmrA is activated under Mg2+ limiting growth conditions or upon exposure to cationic antimicrobial peptides. Under these conditions PmrA activation is mediated by a second two-component system, PhoP/PhoQ. activation of PhoP in Salmonella induces the synthesis of PmrD, which regulates PmrA activity post-transcriptionally by preventing dephosphorylation of PmrA
metabolism
the development of a moderate level of colistin resistance in Acinetobacter baumannii requires distinct genetic events, including (i) at least one point mutation in pmrB, (ii) upregulation of pmrAB, and (iii) expression of pmrC, which lead to addition of phosphoethanolamine to lipid A
metabolism
the PmrA-activated pmrC gene encodes an inner membrane protein that is required for the incorporation of phosphoethanolamine into lipid A and for polymyxin B resistance. The pbg operon and the pmrC genes are solely responsible for PmrA-regulated polymyxin B resistance, but the pmrC gene is dispensable for resistance to Fe3+
metabolism
the PmrA-regulated pmrC gene product mediates the addition of phosphoethanolamine to the 1-position of lipid A and affect resistance to polymxin B, while the PmrA-regulated STM4118 (cptA) gene is necessary for the addition of phosphoethanolamine to the lipopolysacchride core, which is not affected by PmrC, overview. The PmrA-regulated pmrC gene product mediates the addition of phosphoethanolamine to the 1-position of lipid A and affect resistance to polymxin B
metabolism
-
the polymyxin-resistant phenotype is primarily under the control of the PmrA/PmrB two-component regulatory system that is activated during growth under conditions of low pH, high Fe3+, and in a PhoP/PhoQ-dependent manner during Mg2+ starvation
metabolism
the two-component regulatory system PmrA/PmrB controls in part the modifications of the Salmonella enterica serovar Typhimurium lipopolysaccharide with the addition of 4-aminoarabinose to the lipid A and phosphoethanolamine to the lipid A and core in response to the in vivo environment
metabolism
two unlinked PmrA/PmrB-regulated loci, designated pmrE and pmrF, are identified as necessary for resistance of the organism to polymyxin B and for the addition of aminoarabinose to lipid A. Genes immediately flanking this putative operon are also regulated by PmrA/PmrB and/or have been associated with Salmonella typhimurium polymyxin resistance
metabolism
under PmrA regulator activation, the expression of wzzfepE and wzzst genes is induced, and their products are required to determine the O-antigen chain length. Wzzst protein is necessary to maintain the balance of 4-aminoarabinose and phosphoethanolamine lipid A modifications. The interaction of the PmrA-dependent pbgE2 and pbgE3 gene products is important for the formation of the short O-antigen region, protein Wzzst is unable to interact with itself or with the PbgE2 or PbgE3 protein
metabolism
-
PmrA is activated under Mg2+ limiting growth conditions or upon exposure to cationic antimicrobial peptides. Under these conditions PmrA activation is mediated by a second two-component system, PhoP/PhoQ. activation of PhoP in Salmonella induces the synthesis of PmrD, which regulates PmrA activity post-transcriptionally by preventing dephosphorylation of PmrA
-
metabolism
-
the two-component regulatory system PmrA/PmrB controls in part the modifications of the Salmonella enterica serovar Typhimurium lipopolysaccharide with the addition of 4-aminoarabinose to the lipid A and phosphoethanolamine to the lipid A and core in response to the in vivo environment
-
metabolism
-
the PmrA-regulated pmrC gene product mediates the addition of phosphoethanolamine to the 1-position of lipid A and affect resistance to polymxin B, while the PmrA-regulated STM4118 (cptA) gene is necessary for the addition of phosphoethanolamine to the lipopolysacchride core, which is not affected by PmrC, overview. The PmrA-regulated pmrC gene product mediates the addition of phosphoethanolamine to the 1-position of lipid A and affect resistance to polymxin B
-
metabolism
-
under PmrA regulator activation, the expression of wzzfepE and wzzst genes is induced, and their products are required to determine the O-antigen chain length. Wzzst protein is necessary to maintain the balance of 4-aminoarabinose and phosphoethanolamine lipid A modifications. The interaction of the PmrA-dependent pbgE2 and pbgE3 gene products is important for the formation of the short O-antigen region, protein Wzzst is unable to interact with itself or with the PbgE2 or PbgE3 protein
-
metabolism
-
two unlinked PmrA/PmrB-regulated loci, designated pmrE and pmrF, are identified as necessary for resistance of the organism to polymyxin B and for the addition of aminoarabinose to lipid A. Genes immediately flanking this putative operon are also regulated by PmrA/PmrB and/or have been associated with Salmonella typhimurium polymyxin resistance
-
physiological function
enzyme LptA is required for phosphoethanolamine modification of lipid A and contributes to resistance of the organism against the human antimicrobial peptides alpha-defensin and beta-defensin, mechanism of resistance to alpha-defensins, overview. Gene lptA is not required for survival in vivo
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
physiological function
EptA-dependent lipid A modification is required for resistance to polymyxin B, EptA plays a dominant role in polymyxin resistance. Enzyme PmrA is not involved in transcription of LpxT, which catalyses the phosphorylation of lipid A at the 1-position forming 1-diphosphate lipid A increasing the negative charge of the bacterial surface. LpxT-dependent lipid A modification is regulated post-translationally. The regulation does not occur at the level of transcription, but rather following the assembly of LpxT into the inner membrane. PmrA-dependent inhibition of LpxT is required for phosphoethanolamine decoration of lipid A, which is critical for Escherichia coli to resist the bactericidal activity of polymyxin
physiological function
EptA-dependent lipid A modification is required for resistance to polymyxin B. Expression of EptA (PmrC) is under the control of PmrA/PmrB
physiological function
LptA is important for Neisseria gonorrhoeae defence against non-oxidative components produced by polymorphonuclear leukocytes, PMNs. Infection of humans with Neisseria gonorrhoeae is marked by an influx of neutrophils to the site of infection. Enzyme LptA-catalysed modification of lipooligosaccharide enhances gonococcal defence against human neutrophils and enhances survival of the bacteria from the human inflammatory response during acute gonorrhoea. Three mechanisms underlie the increased sensitivity of lptA mutant bacteria to neutrophils: (i) lptA mutant bacteria are more likely to reside in mature phagolysosomes than LptA expressing bacteria, (ii) lptA mutant bacteria are more sensitive to killing by components found in neutrophil granules, including CAP37/azurocidin, human neutrophil peptide 1 and the serine protease cathepsin G, (iii) lptA mutant bacteria are more susceptible to killing by antimicrobial components that are exocytosed from neutrophils, including those decorating neutrophil extracellular traps
physiological function
modification of lipooligosaccharide with phosphoethanolamine by enzyme LptA enhances meningococcal adhesion to human endothelial and epithelial cells in unencapsulated Neisseria meningitidis. LptA does not directly act as an adhesin molecule. Enzyme LptA-mediated adhesion may be masked when meningococci are encapsulated
physiological function
modification of the 1-phosphate group of Helicobacter pylori lipid A requires two enzymatic steps
physiological function
phosphoethanolamine modification of lipid A in colistin-resistant variants of Acinetobacter baumannii, e.g. strain ATCC 19606, is mediated by the pmrAB two-component regulatory system
physiological function
-
phosphoethanolamine-lipid A contributes to serum resistance by modulating factor H binding
physiological function
PmrAB is the global regulatory system that controls lipopolysaccharide modification, leading to a coordinate regulation of 4-aminoarabinose incorporation and O-antigen chain length to respond against the host defense mechanisms. The PmrAB two-component system consists of the PmrA response regulator and the PmrB sensor, which is able to sense Fe3+, activating the system. The PmrAB two-component system activation promotes a remodeling of lipid A and the core region by addition of 4-aminoarabinose and/or phosphoethanolamine. These PmrA-dependent activities are produced by activation of ugd, pbgPE, pmrC, cpta, and pmrG transcription. Lipid A profiles from wild-type and mutant strains, overview
physiological function
the addition of PEA to lipid A by lipid A PEA transferase, LptA, is a major mechanism for resistance to polymyxin in Neisseria meningitidis since this species does not synthesize 4-aminoarabinose. The neisserial lipooligosaccharide phosphoethanolamine transferase A is required for resistance to polymyxin
physiological function
the enzyme EptC serves a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain lipooligosaccharide with a pEtN residue
physiological function
the enzyme EptC serves a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain lipooligosaccharide with a pEtN residue. The enzyme also catalyzes the addition of phosphoethanolamine to the first heptose sugar of the inner core oligosaccharide of lipooligosaccharide, a fourth enzymatic target. Modification of Campylobacter jejuni lipid A with phosphoethanolamine results in increased recognition by the human Toll-like receptor 4-myeloid differentiation factor 2 complex, along with providing resistance to relevant mammalian and avian antimicrobial peptides (i.e., defensins). Modification of surface structures with phosphoethanolamine by EptC is key to its ability to promote commensalism in an avian host and to survive in the mammalian gastrointestinal environment. Modification of FlgG is required for efficient flagellar production and motility
physiological function
the enzyme is responsible for the transfer of phosphoethanolamine residues to the lipid A in several Neisseria meningitidis strains. In all meningococcal strains examined, each lipid A species contains the basal diphosphorylated species, wherein a phosphate group is attached to each glucosamine residue. Also elaborated within the population of lipopolysacchride molecules are a variety of phosphoforms that contain either an additional phosphate residue, an additional phosphoethanolamine residue, additional phosphate and phosphoethanolamine residues, or an additional phosphate and two phosphoethanolamine residues in the lipid A, mass spectroscopic analyses, overview
physiological function
the enzyme modifies two periplasmic targets, a membrane lipid A and a flagellar protein. It is required for efficient motility and flagella production
physiological function
the enzyme phosphoethanolamine transferase A is involved in the addition of phosphoethanolamine moieties to lipid A
physiological function
-
the enzyme regulates the modification of phosphate moieties of lipid A, which may be substituted with L-4-aminoarabinose or phosphoethanolamine groups
physiological function
-
the enzyme regulates the modification of phosphate moieties of lipid A, which may be substituted with L-4-aminoarabinose or phosphoethanolamine groups. The enzyme also regulates the catalysis of periplasmic addition of L-4-aminoarabinose to lipid A through glycosyltransferase L-4-aminoarabinose transferase (ArnT)
physiological function
the PmrA-regulated pmrC gene product mediates the addition of phosphoethanolamine to the 1-position of lipid A and affect resistance to polymxin B
physiological function
the PmrA/PmrB regulatory system of Salmonella enterica controls the modification of lipid A with aminoarabinose and phosphoethanolamine, the PmrA-dependent modification of lipid A with aminoarabinose and phosphoethanolamine is responsible for PmrA-regulated polymyxin B resistance
physiological function
the two-component regulatory system PmrA/PmrB controls in part the modifications of the Salmonella enterica serovar Typhimurium lipopolysaccharide with the addition of 4-aminoarabinose to the lipid A and phosphoethanolamine to the lipid A and core in response to the in vivo environment
physiological function
Cronobacter sakazakii modifies its lipid A structure through the enzyme to avoid recognition by the host immune cells. Gene ESA_RS09200, encodes a phosphoethanolamine transferase that specifically adds a phosphoethanolamine to the 4'-phosphate residue of lipid A, but is not regulated by the PmrA-PmrB system. The enzyme is active in cells grown at pH 5.0, not pH 7.0. Gene ESA_RS09200, but not ESA_RS16425, is required for phosphoethanolamine addition to the lipid A in strain BAA894
physiological function
Gram-negative bacteria survive harmful environmental stressors by modifying their outer membrane. Much of this protection is afforded upon remodeling of the lipid A region of the major surface molecule lipopolysaccharide. Addition of cationic substituents, such as 4-amino-4-deoxy-L-arabinose (L-Ara4N) and phosphoethanolamine (pEtN) at the lipid A phosphate groups, is often induced in response to specific environmental flux stabilizing the outer membrane. ColR specifically induces pEtN addition to lipid A in lieu of L-Ara4N when Zn2+ is present
physiological function
-
wild-type Neisseria gonorrhoeae strain FA1090 has a survival advantage relative to a PEA transferase A (lptA) mutant in the human urethral-challenge and murine lower genital tract infection models. Wild-type lipid A stimulates the humanTLR4-MD2-CD14 complex
physiological function
in Shigella flexneri serotype X and 4a variants called Xv and 4av, respectively, O-antigen modification with phosphoethanolamine (PEtN) is identified, which is encoded by a plasmid-borne gene lpt-O for a PEtN-transferase and confers the monoclonal antibody IV-1(MASF IV-1) determinant to the bacteria. A correlation between the serotype-specific PEtN modification pattern and the lpt-O variation in different serotypes: lpt-ORII in serotype Xv is better tuned for phosphorylation of RhaII and lpt-ORIII in serotypes Yv and 4av for phosphorylation of RhaII
physiological function
phosphoethanolamine transferase LptA in Haemophilus ducreyi modifies lipid A and contributes to human defensin resistance in vitro. The PEA transferase genes confer resistance to alpha and beta-defensins but not to cathelicidin or human serum. Genes lptA is not required for survival in vivo
physiological function
the enzyme is required for substitution of osmoregulated periplasmic glucans by phosphoethanolamine
physiological function
A0A3Z8TVG8
the foodborne enteric pathogen Campylobacter jejuni decorates a variety of its cell-surface structures with phosphoethanolamine. Modifying lipid A with phosphoethanolamine promotes cationic antimicrobial peptide resistance. Modifications of the Campylobacter jejuni surface structures with phosphoethanolamine promote flagellar assembly, motility, cationic antimicrobial peptide resistance and host intestinal colonization
physiological function
the paradigm of resistance to antibiotic colistin mediated by ethanolamine phosphotransferase in Shewanella algae MARS 14. Resistance to colistin in Shewanella algae MARS 14 is associated with overexpression of enzyme EptA (27fold increase), which plays a crucial role in the arrangement of outer membrane lipopolysaccharide
physiological function
LptA functions to transport lipopolysaccharide (LPS) through the periplasm to the outer leaflet of the outer membrane after ABC transporter MsbA flips LPS across the inner membrane. It is hypothesized that LPS binds to LptA to cross the periplasm and that the acyl chains of LPS bind to the central pocket of LptA
physiological function
the enzyme is involved in lipopolysaccharide (LPS) transport. LptA binds lipid A, it might act as a chaperone, assisting the amphipathic LPS molecules to pass through the aqueous periplasm. LptB, LptC, LptF, LptG, and LptH(LptA) are essential components of the LPS transport system in the important model organism for outer membrane biogenesis, Neisseria meningitidis, as they are in Escherichia coli. LptA binds to LptC but not to LptE
physiological function
the LPS (lipopolysaccharide) transport (Lpt) system, a coordinated seven-subunit protein complex that spans the cellular envelope. LPS transport is driven by an ATPase-dependent mechanism dubbed the PEZ model, whereby a continuous stream of LPS molecules is pushed from subunit to subunit, functional significance of LptA oligomerization and LptC. The membrane-bound LptB, F, G and C subunits are connected to the LptD/E heterodimer in the outer membrane by periplasmic LptA. The LptB2FG tetramer extracts LPS from the outer leaflet of the inner membrane and provides the energy to drive LPS transport through an ATPase-dependent mechanism. LptA provides a continuous LPS binding surface that conveys it to the outer membrane. Mechanism of the LPS (lipopolysaccharide) transport (Lpt) system, specific LPS interactions with LptA and LptC, LptC is the intermediate between the inner membrane complex and LptA, overview
physiological function
a 6-residue-requiring zinc-binding/catalytic motif is essential for MCR2-mediated colistin resistance. The transmembrane regions TM2 and TM1 play a critical role in MCR2-mediated colistin resistance, catalytic activity depends on the correct location of MCR2 in bacterial periplasm
physiological function
expression in Escherichia coli leads to 4fold increase in resistance to antibiotics colistin and polymyxin B. In addition to the catalytoc domain, the N-terminal transmembrane regions are required to confer drug resistance in the cell
physiological function
-
gene product of ESA_RS09200 in Cronobacter sakazakii encodes a phosphoethanolamine transferase that specifically adds a phosphoethanolamine to the 4'-phosphate residue of lipid A, but is not regulated by the PmrA-PmrB system. phosphoethanolamine modification of lipid A reduces recognition and killing by the host innate immune system
physiological function
-
minimum inhibitory concentrations of polymyxin B and colistin for the wild-type are twice as high as those for the mutant lacking the eptA gene
physiological function
-
phosphatidylethanolamine is transferred to lipid A by EptA homologue, PetL, and is transferred to galactose by a phosphatidylethanolamine transferase that is unique to Pasteurella multocida called PetG. The presence of a functional petL and petK, which iis responsible for PEtn addition to the single Kdo molecul, an therefore the presence of phosphatidylethanolamine on lipid A and Kdo1, i essential for resistance to the antimicrobial peptide cathelicidin-2. An enzyme inactivation mutant grows similar to wild-type
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
-
physiological function
-
the paradigm of resistance to antibiotic colistin mediated by ethanolamine phosphotransferase in Shewanella algae MARS 14. Resistance to colistin in Shewanella algae MARS 14 is associated with overexpression of enzyme EptA (27fold increase), which plays a crucial role in the arrangement of outer membrane lipopolysaccharide
-
physiological function
-
the enzyme phosphoethanolamine transferase A is involved in the addition of phosphoethanolamine moieties to lipid A
-
physiological function
-
phosphatidylethanolamine is transferred to lipid A by EptA homologue, PetL, and is transferred to galactose by a phosphatidylethanolamine transferase that is unique to Pasteurella multocida called PetG. The presence of a functional petL and petK, which iis responsible for PEtn addition to the single Kdo molecul, an therefore the presence of phosphatidylethanolamine on lipid A and Kdo1, i essential for resistance to the antimicrobial peptide cathelicidin-2. An enzyme inactivation mutant grows similar to wild-type
-
physiological function
-
EptA-dependent lipid A modification is required for resistance to polymyxin B. Expression of EptA (PmrC) is under the control of PmrA/PmrB
-
physiological function
-
the PmrA-regulated pmrC gene product mediates the addition of phosphoethanolamine to the 1-position of lipid A and affect resistance to polymxin B
-
physiological function
-
the two-component regulatory system PmrA/PmrB controls in part the modifications of the Salmonella enterica serovar Typhimurium lipopolysaccharide with the addition of 4-aminoarabinose to the lipid A and phosphoethanolamine to the lipid A and core in response to the in vivo environment
-
physiological function
-
gene product of ESA_RS09200 in Cronobacter sakazakii encodes a phosphoethanolamine transferase that specifically adds a phosphoethanolamine to the 4'-phosphate residue of lipid A, but is not regulated by the PmrA-PmrB system. phosphoethanolamine modification of lipid A reduces recognition and killing by the host innate immune system
-
physiological function
-
Cronobacter sakazakii modifies its lipid A structure through the enzyme to avoid recognition by the host immune cells. Gene ESA_RS09200, encodes a phosphoethanolamine transferase that specifically adds a phosphoethanolamine to the 4'-phosphate residue of lipid A, but is not regulated by the PmrA-PmrB system. The enzyme is active in cells grown at pH 5.0, not pH 7.0. Gene ESA_RS09200, but not ESA_RS16425, is required for phosphoethanolamine addition to the lipid A in strain BAA894
-
physiological function
-
the enzyme is involved in lipopolysaccharide (LPS) transport. LptA binds lipid A, it might act as a chaperone, assisting the amphipathic LPS molecules to pass through the aqueous periplasm. LptB, LptC, LptF, LptG, and LptH(LptA) are essential components of the LPS transport system in the important model organism for outer membrane biogenesis, Neisseria meningitidis, as they are in Escherichia coli. LptA binds to LptC but not to LptE
-
physiological function
-
wild-type Neisseria gonorrhoeae strain FA1090 has a survival advantage relative to a PEA transferase A (lptA) mutant in the human urethral-challenge and murine lower genital tract infection models. Wild-type lipid A stimulates the humanTLR4-MD2-CD14 complex
-
physiological function
-
LptA is important for Neisseria gonorrhoeae defence against non-oxidative components produced by polymorphonuclear leukocytes, PMNs. Infection of humans with Neisseria gonorrhoeae is marked by an influx of neutrophils to the site of infection. Enzyme LptA-catalysed modification of lipooligosaccharide enhances gonococcal defence against human neutrophils and enhances survival of the bacteria from the human inflammatory response during acute gonorrhoea. Three mechanisms underlie the increased sensitivity of lptA mutant bacteria to neutrophils: (i) lptA mutant bacteria are more likely to reside in mature phagolysosomes than LptA expressing bacteria, (ii) lptA mutant bacteria are more sensitive to killing by components found in neutrophil granules, including CAP37/azurocidin, human neutrophil peptide 1 and the serine protease cathepsin G, (iii) lptA mutant bacteria are more susceptible to killing by antimicrobial components that are exocytosed from neutrophils, including those decorating neutrophil extracellular traps
-
physiological function
-
the enzyme regulates the modification of phosphate moieties of lipid A, which may be substituted with L-4-aminoarabinose or phosphoethanolamine groups
-
physiological function
-
the enzyme EptC serves a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain lipooligosaccharide with a pEtN residue. The enzyme also catalyzes the addition of phosphoethanolamine to the first heptose sugar of the inner core oligosaccharide of lipooligosaccharide, a fourth enzymatic target. Modification of Campylobacter jejuni lipid A with phosphoethanolamine results in increased recognition by the human Toll-like receptor 4-myeloid differentiation factor 2 complex, along with providing resistance to relevant mammalian and avian antimicrobial peptides (i.e., defensins). Modification of surface structures with phosphoethanolamine by EptC is key to its ability to promote commensalism in an avian host and to survive in the mammalian gastrointestinal environment. Modification of FlgG is required for efficient flagellar production and motility
-
physiological function
-
the enzyme EptC serves a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain lipooligosaccharide with a pEtN residue
-
physiological function
-
the foodborne enteric pathogen Campylobacter jejuni decorates a variety of its cell-surface structures with phosphoethanolamine. Modifying lipid A with phosphoethanolamine promotes cationic antimicrobial peptide resistance. Modifications of the Campylobacter jejuni surface structures with phosphoethanolamine promote flagellar assembly, motility, cationic antimicrobial peptide resistance and host intestinal colonization
-
physiological function
-
minimum inhibitory concentrations of polymyxin B and colistin for the wild-type are twice as high as those for the mutant lacking the eptA gene
-
physiological function
-
phosphoethanolamine transferase LptA in Haemophilus ducreyi modifies lipid A and contributes to human defensin resistance in vitro. The PEA transferase genes confer resistance to alpha and beta-defensins but not to cathelicidin or human serum. Genes lptA is not required for survival in vivo
-
physiological function
-
PmrAB is the global regulatory system that controls lipopolysaccharide modification, leading to a coordinate regulation of 4-aminoarabinose incorporation and O-antigen chain length to respond against the host defense mechanisms. The PmrAB two-component system consists of the PmrA response regulator and the PmrB sensor, which is able to sense Fe3+, activating the system. The PmrAB two-component system activation promotes a remodeling of lipid A and the core region by addition of 4-aminoarabinose and/or phosphoethanolamine. These PmrA-dependent activities are produced by activation of ugd, pbgPE, pmrC, cpta, and pmrG transcription. Lipid A profiles from wild-type and mutant strains, overview
-
additional information
analysis of the three-dimensional structure of the soluble catalytic domain of LptA, active-site residues, structure homology, overview
additional information
analysis of the three-dimensional structure of the soluble catalytic domain of LptA, active-site residues, structure homology, overview
additional information
-
analysis of the three-dimensional structure of the soluble catalytic domain of LptA, active-site residues, structure homology, overview
additional information
homology structure modeling of the enzyme, active-site residues and metal binding structures, crystal structure analysis, overview
additional information
homology structure modeling of the enzyme, active-site residues and metal binding structures, crystal structure analysis, overview
additional information
-
homology structure modeling of the enzyme, active-site residues and metal binding structures, crystal structure analysis, overview
additional information
A0A3Z8TVG8
identification of identify zinc-ligand residues, a putative nucleophile and conserved active-site residues required for in vivo activity from the crystal structure, active-site architecture of cEptC, overview
additional information
-
identification of identify zinc-ligand residues, a putative nucleophile and conserved active-site residues required for in vivo activity from the crystal structure, active-site architecture of cEptC, overview
additional information
-
homology structure modeling of the enzyme, active-site residues and metal binding structures, crystal structure analysis, overview
-
additional information
-
identification of identify zinc-ligand residues, a putative nucleophile and conserved active-site residues required for in vivo activity from the crystal structure, active-site architecture of cEptC, overview
-
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H358A
A0A3Z8TVG8
site-directed mutagenesis, mutation of a potential zinc binding residue
H440A
A0A3Z8TVG8
site-directed mutagenesis, mutation of a potential zinc binding residue
N308A
A0A3Z8TVG8
site-directed mutagenesis, mutation of a potential zinc binding residue
S309A
A0A3Z8TVG8
site-directed mutagenesis, mutation of a potential zinc binding residue
T266A
A0A3Z8TVG8
site-directed mutagenesis, mutation of a potential zinc binding residue
T266S
A0A3Z8TVG8
site-directed mutagenesis, mutation of a potential zinc binding residue
H358A
-
site-directed mutagenesis, mutation of a potential zinc binding residue
-
H440A
-
site-directed mutagenesis, mutation of a potential zinc binding residue
-
N308A
-
site-directed mutagenesis, mutation of a potential zinc binding residue
-
S309A
-
site-directed mutagenesis, mutation of a potential zinc binding residue
-
T266S
-
site-directed mutagenesis, mutation of a potential zinc binding residue
-
D463A
mutant cannot confer robust growth to the recipient strain in presence of more than 2 mg/liter of colistin
E244A
mutant cannot confer robust growth to the recipient strain in presence of more than 2 mg/liter of colistin
H393A
mutant cannot confer robust growth to the recipient strain in presence of more than 2 mg/liter of colistin
H464A
mutant cannot confer robust growth to the recipient strain in presence of more than 2 mg/liter of colistin
H476A
mutant cannot confer robust growth to the recipient strain in presence of more than 2 mg/liter of colistin
I36R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
I36R1/Q148A/K149A
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
I86R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
I86R1/Q148A/K149A
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
L145R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
L45R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
M98R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
N185R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
N185R1/Q148A/K149A
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
Q148A/K149A
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
S110R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
T283A
mutant cannot confer robust growth to the recipient strain in presence of more than 2 mg/liter of colistin
T32R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
V132R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
V165R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
T315A
mutation of the catalytic domain, abolishes antibiotic resistance activity
additional information
construction of several enzyme mutant strains, overview
additional information
generation of a mutant in Campylobacter jejuni 81-176 by interruption of cj0256 results in the absence of pEtN modifications on lipid A as well as FlgG
additional information
-
generation of a mutant in Campylobacter jejuni 81-176 by interruption of cj0256 results in the absence of pEtN modifications on lipid A as well as FlgG
additional information
-
construction of several enzyme mutant strains, overview
-
additional information
construction of Cronobacter sakazakii mutant strains WLL001, a ESA_RS09200 deletion mutant, and of WLL002, WLL003 and WLL004, with mutationsof genes lpxE, ESA-RS16430, and ESA_RS16425, with or without additional deletion of ESA_RS09200. Analysis of mammalian cell invasion abilities of mutants using human enterocyte-like epithelial Caco-2 cells, overview
additional information
-
construction of Cronobacter sakazakii mutant strains WLL001, a ESA_RS09200 deletion mutant, and of WLL002, WLL003 and WLL004, with mutationsof genes lpxE, ESA-RS16430, and ESA_RS16425, with or without additional deletion of ESA_RS09200. Analysis of mammalian cell invasion abilities of mutants using human enterocyte-like epithelial Caco-2 cells, overview
additional information
-
construction of Cronobacter sakazakii mutant strains WLL001, a ESA_RS09200 deletion mutant, and of WLL002, WLL003 and WLL004, with mutationsof genes lpxE, ESA-RS16430, and ESA_RS16425, with or without additional deletion of ESA_RS09200. Analysis of mammalian cell invasion abilities of mutants using human enterocyte-like epithelial Caco-2 cells, overview
-
additional information
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generation of polymyxin-sensitive mutants of an Escherichia coli pmrAC strain WD101 producing a lipid A that lacked both the 3'-acyloxyacyl-linked myristate (C14) and L-4-aminoarabinose, even though the necessary enzymatic machinery required to synthesize L-4-aminoarabinose-modified lipid A is present. Strain WD103 is generated by P1vir transduction of the polymyxin-resistant genotype (pmrAC) of strain WD101 into the Escherichia coli lpxM mutant MLK1067, phenotype, overview. The polymyxin-sensitive parent strains MLK1067 and W3110 produce unmodified penta- or hexa-acylated lipid A, respectively. Complementation of WD103 with the vector pWSLpxM resulted in restoration of polymyxin resistance to the levels displayed by WD101, effect of lipid myristoylation on the polymyxin resistance
additional information
construction of the opgE::cml mutant, and of the opgE::Tn5 mutant by random transposon mutagenesis with Tn5
additional information
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construction of the opgE::cml mutant, and of the opgE::Tn5 mutant by random transposon mutagenesis with Tn5
additional information
domain swapping between isoforms Mcr1 and Mcr2 shows that the presence of the resultant two chimeric genes can confer resistance of the colistin-susceptible strain MG1655 to up to 16 mg/liter of colistin
additional information
construction of gene lptA mutant and complement strains from strain FA 1090
additional information
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construction of gene lptA mutant and complement strains from strain FA 1090
additional information
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piliated colony variants of strain FA19 are transformed with plasmid or chromosomal DNA preparations bearing insertionally inactivated lpt3, lpt6, or lptA genes prepared previously from Neisseria meningitidis strain NMB
additional information
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construction of a leptA knockout mtant
additional information
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construction of a leptA knockout mtant
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additional information
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construction of gene lptA mutant and complement strains from strain FA 1090
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additional information
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piliated colony variants of strain FA19 are transformed with plasmid or chromosomal DNA preparations bearing insertionally inactivated lpt3, lpt6, or lptA genes prepared previously from Neisseria meningitidis strain NMB
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additional information
construction of a membrane-deletion mutant of the enzyme
additional information
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construction of a membrane-deletion mutant of the enzyme
additional information
construction of insertional lptA mutants from 35E (L2), H44/76 (L3), and 89I (L4) backgrounds
additional information
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construction of insertional lptA mutants from 35E (L2), H44/76 (L3), and 89I (L4) backgrounds
additional information
generation of a soluble enzyme mutant by deletion of the membrane binding structure. The mutant does not confer resistance to polymyxin in transformed Escherichia coli cells, in contrast to the wild-type LptA
additional information
generation of a soluble enzyme mutant by deletion of the membrane binding structure. The mutant does not confer resistance to polymyxin in transformed Escherichia coli cells, in contrast to the wild-type LptA
additional information
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generation of a soluble enzyme mutant by deletion of the membrane binding structure. The mutant does not confer resistance to polymyxin in transformed Escherichia coli cells, in contrast to the wild-type LptA
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
additional information
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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
additional information
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generation of a soluble enzyme mutant by deletion of the membrane binding structure. The mutant does not confer resistance to polymyxin in transformed Escherichia coli cells, in contrast to the wild-type LptA
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additional information
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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
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additional information
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construction of a membrane-deletion mutant of the enzyme
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additional information
lipid A prepared from the PA14DELTAeptAPa mutant shows no phosphatidylethanolamine modification when Zn2+ is added to the media
additional information
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lipid A prepared from the PA14DELTAeptAPa mutant shows no phosphatidylethanolamine modification when Zn2+ is added to the media
additional information
JSG435 carries a mutant pmrA locus allele (pmrA505), JSG435 is mutagenized with the transposon Tn10d. Chromosomal mapping of the transposon insertions of the two polymyxin B sensitive strains shows them to be located at 50-52 centisomes (JSG485) and 43-45 centisomes (JSG486), thus eliminating the possibility that mutations in these regulatory loci are responsible for the observed phenotypic change
additional information
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JSG435 carries a mutant pmrA locus allele (pmrA505), JSG435 is mutagenized with the transposon Tn10d. Chromosomal mapping of the transposon insertions of the two polymyxin B sensitive strains shows them to be located at 50-52 centisomes (JSG485) and 43-45 centisomes (JSG486), thus eliminating the possibility that mutations in these regulatory loci are responsible for the observed phenotypic change
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additional information
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construction of a pmrA- null mutant strain JSG421 of covalently modified pmrAc strains JSG485 and JSG486, overview
additional information
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construction of a pmrA- null mutant strain JSG421 of covalently modified pmrAc strains JSG485 and JSG486, overview
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additional information
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generation of an lptA deletion mutant strain using plasmid pMEB256, with or without combined deletions of genes ptdA and ptdB
additional information
generation of an lptA deletion mutant strain using plasmid pMEB256, with or without combined deletions of genes ptdA and ptdB
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Herrera, C.M.; Hankins, J.V.; Trent, M.S.
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Neisseria gonorrhoeae, Neisseria gonorrhoeae FA19
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Campylobacter jejuni (A0A3X8T8A0), Campylobacter jejuni 81-176 (A0A3X8T8A0)
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Neisseria meningitidis (X5ELY0), Neisseria meningitidis
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The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica
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Salmonella enterica (Q8Z1P4)
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Salmonella enterica (P36555), Salmonella enterica (Q8Z1P4), Salmonella enterica LT2 (P36555), Salmonella enterica LT2 (Q8Z1P4)
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Zhou, Z.; Ribeiro, A.A.; Lin, S.; Cotter, R.J.; Miller, S.I.; Raetz, C.R.
Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation
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Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
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Tran, A.X.; Karbarz, M.J.; Wang, X.; Raetz, C.R.H.; McGrath, S.C.; Cotter, R.J.; Trent, M.S.
Periplasmic cleavage and modification of the 1-phosphate group of Helicobacter pylori lipid A
J. Biol. Chem.
279
55780-55791
2004
Helicobacter pylori (O24867), Helicobacter pylori
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Tran, A.X.; Lester, M.E.; Stead, C.M.; Raetz, C.R.; Maskell, D.J.; McGrath, S.C.; Cotter, R.J.; Trent, M.S.
Resistance to the antimicrobial peptide polymyxin requires myristoylation of Escherichia coli and Salmonella typhimurium lipid A
J. Biol. Chem.
280
28186-28194
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Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium C5
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Cullen, T.W.; Madsen, J.A.; Ivanov, P.L.; Brodbelt, J.S
Trent, M.S.: Characterization of unique modification of flagellar rod protein FlgG by Campylobacter jejuni lipid A phosphoethanolamine transferase, linking bacterial locomotion and antimicrobial peptide resistance
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287
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Campylobacter jejuni (A0A3X8T8A0), Campylobacter jejuni, Campylobacter jejuni 81-176 (A0A3X8T8A0)
brenda
Farizano, J.V.; Pescaretti, M.d.e..L.; Lopez, F.E.; Hsu, F.F.; Delgado, M.A.
The PmrAB system-inducing conditions control both lipid A remodeling and O-antigen length distribution, influencing the Salmonella typhimurium-host interactions
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Salmonella enterica (Q8Z1P4), Salmonella enterica 14028s (Q8Z1P4)
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Wanty, C.; Anandan, A.; Piek, S.; Walshe, J.; Ganguly, J.; Carlson, R.W.; Stubbs, K.A.; Kahler, C.M.; Vrielink, A.
The structure of the neisserial lipooligosaccharide phosphoethanolamine transferase A (LptA) required for resistance to polymyxin
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425
3389-3402
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Neisseria meningitidis (Q7DD94), Neisseria meningitidis (Q7DDQ9), Neisseria meningitidis, Neisseria meningitidis NMB (Q7DDQ9)
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Gunn, J.S.; Lim, K.B.; Krueger, J.; Kim, K.; Guo, L.; Hackett, M.; Miller, S.I.
PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance
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27
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Salmonella enterica (Q8Z1P4), Salmonella enterica 14028s (Q8Z1P4)
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Trombley, M.P.; Post, D.M.; Rinker, S.D.; Reinders, L.M.; Fortney, K.R.; Zwickl, B.W.; Janowicz, D.M.; Baye, F.M.; Katz, B.P.; Spinola, S.M.; Bauer, M.E.
Phosphoethanolamine transferase LptA in Haemophilus ducreyi modifies lipid A and contributes to human defensin resistance in vitro
PLoS ONE
10
e0124373
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[Haemophilus] ducreyi, [Haemophilus] ducreyi (Q7VMW0), [Haemophilus] ducreyi ATCC 700724 (Q7VMW0)
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Cullen, T.; Trent, M.
A link between the assembly of flagella and lipooligosaccharide of the gram-negative bacterium Campylobacter jejuni
Proc. Natl. Acad. Sci. USA
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Campylobacter jejuni (A0A3X8T8A0), Campylobacter jejuni
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Packiam, M.; Yedery, R.D.; Begum, A.A.; Carlson, R.W.; Ganguly, J.; Sempowski, G.D.; Ventevogel, M.S.; Shafer, W.M.; Jerse, A.E.
Phosphoethanolamine decoration of Neisseria gonorrhoeae lipid A plays a dual immunostimulatory and protective role during experimental genital tract infection
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Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
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Liu, L.; Li, Y.; Wang, X.; Guo, W.
A phosphoethanolamine transferase specific for the 4'-phosphate residue of Cronobacter sakazakii lipid A
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Cronobacter sakazakii (A7MFE0), Cronobacter sakazakii, Cronobacter sakazakii BAA894 (A7MFE0)
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Extracellular zinc induces phosphoethanolamine addition to Pseudomonas aeruginosa lipid A via the ColRS two-component system
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The role of oxidoreductases in determining the function of the neisserial lipid A phosphoethanolamine transferase required for resistance to polymyxin
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Crystallographic study of the phosphoethanolamine transferase EptC required for polymyxin resistance and motility in Campylobacter jejuni
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Neisseria meningitidis serogroup B (Q7DD94), Neisseria meningitidis serogroup B MC58 (Q7DD94)
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Escherichia coli, Escherichia coli Nissle 1917
-
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van t Hag, L.; Anandan, A.; Seabrook, S.A.; Gras, S.L.; Drummond, C.J.; Vrielink, A.; Conn, C.E.
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Neisseria meningitidis serogroup B (Q7DD94), Neisseria meningitidis serogroup B MC58 (Q7DD94)
brenda