Any feedback?
Information on EC 2.7.8.43 - lipid A phosphoethanolamine transferase
for references in articles please use BRENDA:EC2.7.8.43Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.8.43 lipid A phosphoethanolamine transferaseIUBMB Comments
The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-beta-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.
Specify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
phosphoethanolamine transferase, petn transferase, pea transferase, lipid a phosphoethanolamine transferase, cj0256, esa_rs09200, lipooligosaccharide phosphoethanolamine transferase a, hp0022, lpt-o, petn-transferase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A0R63_06305
Cj0256
EC 2.7.4.30
-
-
formerly
-
EptA
EptC
ESA_RS09200
ethanolamine phosphotransferase
HD_0852
lipid A PEA transferase
lipid A phosphoethanolamine transferase
lipooligosaccharide phosphoethanolamine transferase A
LOS PEA transferase A
LptA
LptH
NMB1638
NmLptA
PEA transferase
PEA transferase A
PetL
pEtN transferase
phosphoethanolamine transferase
phosphoethanolamine transferase A
PmrA
PmrC
polymyxin resistance protein A
polymyxin resistance protein C
sNMLptA
lipid A PEA transferase
-
-
-
-
LptA
-
-
-
-
PmrA
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diacylphosphatidylethanolamine + lipid A 1-(2-aminoethyl diphosphate) = diacylglycerol + lipid A 1,4'-bis(2-aminoethyl diphosphate)
(3)
-
-
-
diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
(1)
-
-
-
diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
(2)
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
diacylphosphatidylethanolamine:lipid-A phosphoethanolaminetransferase
The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-beta-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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)
-
?
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
?
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)
[Haemophilus] ducreyi ATCC 700724
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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)
[Haemophilus] ducreyi ATCC 700724
-
-
-
?
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
-
?
additional information
?
-
addition of phosphoethanolamine to hepta-acylated lipid A
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
A0A3Z8TVG8
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
-
-
?
additional information
?
-
-
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
-
-
?
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
-
-
?
additional information
?
-
A0A3Z8TVG8
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
-
-
?
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
-
-
?
additional information
?
-
the phosphoethanolamine cycle, overview
-
-
?
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
-
-
?
additional information
?
-
specific LPS interactions with LptA and LptC
-
-
?
additional information
?
-
transfer may occur both to the 4'- and 1-phospho groups of lipid A
-
-
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
?
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
NMR spectroscopic analysis of O-antigen substrates and products, detailed overview
-
-
?
additional information
?
-
-
NMR spectroscopic analysis of O-antigen substrates and products, detailed overview
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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)
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
A0A3Z8TVG8
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
?
A0A3Z8TVG8
-
-
-
?
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)
-
-
-
?
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
-
-
?
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 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)
-
-
-
?
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
-
-
?
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
-
-
?
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)
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
A0A3Z8TVG8
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
-
-
?
additional information
?
-
-
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
-
-
?
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
-
-
?
additional information
?
-
A0A3Z8TVG8
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
-
-
?
additional information
?
-
the phosphoethanolamine cycle, overview
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe3+
required, the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+
Mg2+
Zn2+
additional information
Mg2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases
Mg2+
required, two Mg2+ ions per enzyme molecule, binding structure model
Zn2+
A0A3Z8TVG8
zinc-binding residues of the phosphoenzyme intermediate, overview. The cEptC active site contains a tetrahedrally coordinated zinc ion and a putative nucleophilic threonine, Thr266, covalently bound to a phosphoryl group to form phosphothreonine
Zn2+
a zinc ion is present at a conserved site in addition to three zincs more peripherally located in the active site
Zn2+
metal ions present in the active site are coordinated to Thr280 and to residues conserved among the family of transferases, interaction of the Zn2+ with the active site, binding site structure, overview. The second Zn2+ ion is coordinated by the side chains of His383, His465, and one of the oxygen atoms of the phosphate group attached to Thr280. In LptA, two types of coordination around the Zn1 are observed depending on the state of Thr280. In the case of non-phosphorylated Thr280, the coordination about Zn1 is tetrahedral with the fourth ligand being the free phosphate group. In contrast, when Thr280 is phosphorylated, a penta-coordinated metal is observed with the hydroxyl oxygen atom of Thr280 and one of the phosphate oxygen atoms each interacting weakly with the metal
Zn2+
required, one Zn2+ ion per enzyme molecule coordinated tetrahedrally by the side chains of Glu240, Asp452, and His453 and the hydroxyl oxygen atom of Thr280, very strong binding to the enzyme, binding structure model
Zn2+
extracellular zinc induces phosphoethanolamine addition to Pseudomonas aeruginosa lipid A via the ColRS two-component system
additional information
three bound metal ions (two Zn2+ and a Mg2+) are implicated in catalysis
additional information
three bound metal ions (two Zn2+ and a Mg2+) are implicated in catalysis
additional information
-
three bound metal ions (two Zn2+ and a Mg2+) are implicated in catalysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
polymyxin
resistance to polymyxin for the enzyme is realized by oxidoreductase DsbA
-
LpxT
role for LpxT in the reduction of enzyme EptA activity, the transcriptional regulation of lpxT gene is PmrA-independent. PmrA-dependent inhibition of LpxT is required for phosphoethanolamine decoration of lipid A
-
LpxT
role for LpxT in the reduction of enzyme EptA activity. Loss of Salmonella lpxT greatly increases modification of lipid A through enzyme EptA. LpxT catalyses the phosphorylation of lipid A at the 1-position
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arbutin
arbutin is also a substrate for phosphoethanolamine transferase stimulating its activity, increasing phosphatidylethanolamine turnover leading to accumulation of diacylglycerol toxic for bacteria
PmrA
te enzyme EptA is activated in a PmrA-dependent manner, overview
-
additional information
the neisserial oxidoreductase, DsbA3, contributes to the activity of LptA
-
additional information
-
the neisserial oxidoreductase, DsbA3, contributes to the activity of LptA
-
additional information
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, mutational analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Ischemia
A comparison of the reversibility of phosphoethanolamine transferase and phosphocholine transferase in rat brain microsomes.
Hypersensitivity
A phosphoethanolamine transferase specific for the outer 3-deoxy-D-manno-octulosonic acid residue of Escherichia coli lipopolysaccharide. Identification of the eptB gene and Ca2+ hypersensitivity of an eptB deletion mutant.
Infections
Modification of lipooligosaccharide with phosphoethanolamine by LptA in Neisseria meningitidis enhances meningococcal adhesion to human endothelial and epithelial cells.
Infections
Phosphoethanolamine Decoration of Neisseria gonorrhoeae Lipid A Plays a Dual Immunostimulatory and Protective Role during Experimental Genital Tract Infection.
Malnutrition
Effects of neonatal undernutrition of rats on the synthesis of phosphatidylcholine and phosphatidylethanolamine by microsomes from gray matter and white matter.
Reproductive Tract Infections
Phosphoethanolamine Decoration of Neisseria gonorrhoeae Lipid A Plays a Dual Immunostimulatory and Protective Role during Experimental Genital Tract Infection.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
diverse colistin sensitive and resistant strains, gene pmrA
UniProt
brenda
a lpxM mutant strain, gene pmrA
-
-
brenda
a colistin-resistant clinical isolate from resistant clinical isolate retrieved from bronchoalveolar lavage of a hospitalised patient
UniProt
brenda
a colistin-resistant clinical isolate from resistant clinical isolate retrieved from bronchoalveolar lavage of a hospitalised patient
UniProt
brenda
[Haemophilus] ducreyi ATCC 700724
human-passaged variant of class I clinical isolate 35000
UniProt
brenda
serogroups A and B, diverse strains, overview, gene lptA
UniProt
brenda
a lpxM mutant strain, gene pmrA
-
-
brenda
human-passaged variant of class I clinical isolate 35000
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
colistin resistant strains show higher enzyme expression compared to colistin sensitive strains, enzyme expression analysis, overview
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
A0A3Z8TVG8
phosphoethanolamine modification occurs on the periplasmic side of the inner membrane, where enzyme EptC transfers head groups from the phospholipid phosphoethanolamine to target molecules. EptC is predicted to be anchored to the inner membrane by a five-helix transmembrane domain, with its sulfatase-like catalytic domain positioned in the periplasm
-
brenda
-
phosphoethanolamine modification occurs on the periplasmic side of the inner membrane, where enzyme EptC transfers head groups from the phospholipid phosphoethanolamine to target molecules. EptC is predicted to be anchored to the inner membrane by a five-helix transmembrane domain, with its sulfatase-like catalytic domain positioned in the periplasm
-
-
brenda
the enzyme is located on the periplasmic side of the inner membrane
-
brenda
LptA is the only component of the Lpt system that lacks a transmembrane component, as it spans the periplasmic space between the inner membrane and outer membrane complexes. LptA is bound to other Lpt components rather than floating freely in the periplasm
-
brenda
possibly one or more LptA proteins bridges the periplasm to form a large, connected protein complex
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
[Haemophilus] ducreyi ATCC 700724
-
deletion of two putative PEA transferase genes in Haemophilus ducreyi increases susceptibility to HBD-3
-
malfunction
-
phenotypes of mutants of PmrA-dependent genes pbgE2 and pbgE3, overview
-
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
[Haemophilus] ducreyi ATCC 700724
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A7MFE0_CROS8
Cronobacter sakazakii (strain ATCC BAA-894)
542
0
60993
TrEMBL
-
EPTA_HELPY
Helicobacter pylori (strain ATCC 700392 / 26695)
521
0
58859
Swiss-Prot
-
LPTA_ECOLI
Escherichia coli (strain K12)
185
0
20127
Swiss-Prot
Secretory Pathway (Reliability: 1)
EPTA_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
547
0
61619
Swiss-Prot
-
Q5F6F3_NEIG1
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
176
0
18344
TrEMBL
-
Q7DD94_NEIMB
Neisseria meningitidis serogroup B (strain MC58)
544
0
61363
TrEMBL
-
Q7DDQ9_NEIMB
Neisseria meningitidis serogroup B (strain MC58)
176
0
18192
TrEMBL
-
Q7VMW0_HAEDU
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
551
0
62886
TrEMBL
-
S4UV19_SHIFL
506
0
58001
TrEMBL
other Location (Reliability: 2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
the enzyme LptA arranges in an end-to-end fibrous tetramer, which forms a continuous hydrophobic groove between the LptA monomers, crystal structure analysis. Mass spectral analysis confirmes that LptA forms 2-5-member oligomers in a concentration-dependent manner when purified in vitro and that the resultant complexes are stabilized by LPS. Analysis of subunit interactions
additional information
additional information
according to light scattering data, LptA oligomerizes in a concentration-dependent manner. LptA is an average of a trimer in solution, and a considerably higher order oligomerization state (25mers) is predicted at a protein concentration of 0.1 mM
additional information
the enzyme is composed of an N-terminal transmembrane domain and a C-terminal soluble domain. Tryptic peptide mapping and analysis by MALDI-TOF/TOF mass spectrometry
additional information
-
the enzyme is composed of an N-terminal transmembrane domain and a C-terminal soluble domain. Tryptic peptide mapping and analysis by MALDI-TOF/TOF mass spectrometry
additional information
secondary-structure ribbon representation of the soluble domain of LptA, and modeling of the three-dimensional structure of LptA, overview. Possible formation of five intramolecular disulfide bonds: Cys276-Cys286, Cys327-Cys331, Cys348-Cys353, Cys402-Cys410, and Cys499-Cys540
additional information
secondary-structure ribbon representation of the soluble domain of LptA, and modeling of the three-dimensional structure of LptA, overview. Possible formation of five intramolecular disulfide bonds: Cys276-Cys286, Cys327-Cys331, Cys348-Cys353, Cys402-Cys410, and Cys499-Cys540
additional information
-
secondary-structure ribbon representation of the soluble domain of LptA, and modeling of the three-dimensional structure of LptA, overview. Possible formation of five intramolecular disulfide bonds: Cys276-Cys286, Cys327-Cys331, Cys348-Cys353, Cys402-Cys410, and Cys499-Cys540
additional information
-
secondary-structure ribbon representation of the soluble domain of LptA, and modeling of the three-dimensional structure of LptA, overview. Possible formation of five intramolecular disulfide bonds: Cys276-Cys286, Cys327-Cys331, Cys348-Cys353, Cys402-Cys410, and Cys499-Cys540
-
additional information
-
the enzyme is composed of an N-terminal transmembrane domain and a C-terminal soluble domain. Tryptic peptide mapping and analysis by MALDI-TOF/TOF mass spectrometry
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
A0A3Z8TVG8
the cEptC active site contains a putative nucleophilic threonine, Thr266, covalently bound to a phosphoryl group to form phosphothreonine. Phospho-Thr266 mimics an enzyme reaction intermediate representing the first step in a two-step transferase reaction
phosphoprotein
-
the cEptC active site contains a putative nucleophilic threonine, Thr266, covalently bound to a phosphoryl group to form phosphothreonine. Phospho-Thr266 mimics an enzyme reaction intermediate representing the first step in a two-step transferase reaction
-
phosphoprotein
phosphorylation of the putative nucleophile, Thr280
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged wild-type and selenomethionine-labeled enzyme EptC, sitting drop vapour diffusion method, mixing of 0.004 ml of 30 mg/ml protein in 25 mM NaCl, 10 mM HEPES, pH 7.5, with 0.001 ml of precipitant solution containing 200 mM diammonium phosphate, 15% w/v PEG 3350, 22°C, X-ray diffraction structure determination and analysis at 2.40-2.80 A resolution, molecular replacement
A0A3Z8TVG8
structure of the catalytic domain ofMCR1 at 1.32 A resolution. The putative nucleophile for catalysis, threonine 285, is phosphorylated in MCR1 and a zinc is present at a conserved site in addition to three zincs more peripherally located in the active site. Binding sites for the lipid A and phosphatidylethanolamine substrates are not apparent in the MCR1 structure
structure of the catalytic domain of ICR.. Catalytic domain dimerization is required for substrate binding. The structure reveals two disulfide bonds (Cys390 to Cys398, Cys448 to Cys456)
purified recombinant His6-tagged soluble catalytic domain of LptA, free and selenomethionine-labeled, or in complex with Zn2+ and a truncated form of substrate 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine, X-ray diffraction structure determination and analysis at 1.43-1.78 A resolution, molecular replacement. and modeling
recombinant His-tagged membrane-deletion mutant enzyme, mixing of 0.001 ml of 5.2 mg/ml protein in 50 mM HEPES, pH 8.0, 50 mM sodium chloride, with 0.001 ml of crystallization solution containing 23-26% PEG 8000, 100 mM ammonium sulfate, 100 mM HEPES, pH 7.58.0, 15 mM n-dodecyl-N,N-dimethylamine-N-oxide, and 200 nl of microseeding solution, 20°C, 3-5 days, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution
structure of full-length lipid A phosphoethanolamine transferase, determined to 2.75 A resolution. The structure reveals a helical membrane domain and a periplasmic facing soluble domain. The domains are linked by a helix that runs along the membrane surface interacting with the phospholipid head groups. Two helices located in a periplasmic loop between two transmembrane helices contain conserved charged residues and are implicated in substrate binding
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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
-
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
-
construction of gene lptA mutant and complement strains from strain FA 1090
additional information
-
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
-
construction of gene lptA mutant and complement strains from strain FA 1090
-
additional information
-
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
construction of a membrane-deletion mutant of the enzyme
additional information
-
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
-
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
-
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
-
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
-
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
-
construction of a membrane-deletion mutant of the enzyme
-
additional information
lipid A prepared from the PA14DELTAeptAPa mutant shows no phosphatidylethanolamine modification when Zn2+ is added to the media
additional information
-
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
-
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
-
construction of a pmrA- null mutant strain JSG421 of covalently modified pmrAc strains JSG485 and JSG486, overview
additional information
-
construction of a pmrA- null mutant strain JSG421 of covalently modified pmrAc strains JSG485 and JSG486, overview
-
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
all three neisserial oxidoreductases, including DsbA1, DsbA2 and DsbA3, contribute to resistance to polymyxin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by cobalt affinity chromatography, dialysis, and ultrafiltration
recombinant His-tagged membrane-deletion mutant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis
recombinant His-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
A0A3Z8TVG8
recombinant His6-tagged enzyme from Escherichi coli strain JCB570 and Neisseria meningitidis by nickel affinity chromatography and ultrafiltration
recombinant protein, purification in the presence of the detergent dodecyl-beta-D-maltoside
recombinant wild-type and selenomethionine-labeled His6-tagged soluble periplasmic domain of the enzyme from Escherichia coli by nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene cj0256, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli K-12 strain W3110/EC01
gene eptA, construction of a pZE21MCS-1 plasmid-based genomic expression library in Escherichia coli strain TOP10, DNA and amino acid sequence determination and analysis, functional EptA enzyme expression in Escherichia coli strain TOP10
gene eptA, quantitative and semi-quantitative reverse-transcriptase (RT) PCR enzyme expression analysis
gene eptC, recombinant expression of C-terminally Gly6-His8-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression of His-tagged enzyme as selenomethionine-labeled enzyme
A0A3Z8TVG8
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, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain W3110
gene HD_0852 or lptA, homology screening and DNA and amino acid sequence determination and analysis
gene Hp0022, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli NovaBlue(DE3) membranes. method optimization
gene lptA
gene lptA, DNA and amino acid sequence determination and analysis, genotyping in Neisseria, recombinant expression of His6-tagged enzyme in Escherichi coli strain JCB570 and in Neisseria meningitidis from low copy expression vector pCMK1001. In Escherichia coli, the stability and activity of neisserial LptA::Hisx6 is entirely dependent upon the coexpression of the EcDsbA oxidoreductase. Although expression of LptA::Hisx6 and EcDsbA in Escherichia coli results in a 32fold increase in polymyxin resistance, the proportion of lipid A headgroups substituted with PEA rises to 26%
gene lptA, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli
gene lptA, expression from a a multicopy plasmid in Neisseria meningitidis, construction of an lptA-FLAG epitope-tagged fusion Neisseria meningitidis strain HT1295 from strain H44/76
gene lptA, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
gene lptA, recombinant expression of wild-type and soluble (membrane-deleted) C-terminally His6-tagged enzyme in Escherichia coli DELTAdsbA mutant strain JCB571 from plasmids pCMK255 and pCMK527, expression of wild-type enzyme confers resistance to polymyxin in Escherichia coli, while expression of the truncated soluble mutant does not
gene pmrA, genetic organization of the pmrCAB genes, PCR-based expression analysis in colistin sensitive and resistant strains
gene pmrA, sequence comparisons with Neisseria meningitidis phosphoethanolamine phosphotransferases lptA, lpt3, and lpt6
genetic screening identifies gene opgE, DNA and amino acid sequence determination and analysis, genetic organization of opg genes in Escherichia coli, overview. The gene is transformed into competent Escherichia coli cells to give pNF752
recombinant expression of His-tagged membrane-deletion mutant enzyme in Escherichia coli strain BL21(DE3)pLysS
recombinant expression of wild-type and selenomethionine-labeled His6-tagged soluble periplasmic domain of the enzyme in Escherichia coli strains CKEC272 and CKEC580
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of EptA (PmrC) is under the control of PmrA/PmrB
PetL expression is positively regulated by the global regulator Fis and negatively regulated by an Hfq-dependent small RNA
the peptA (eptA promoter) is induced sevenfold in the presence of Fe3+, induction is lost in enzyme mutant strain CH020 (DELTApmrA)
transcription of the enzyme eptAPa is regulated by zinc via the ColRS two-component system. The two-component system response regulator ColR activates eptAPa transcription. Transcription of eptAPa is induced by 2 mM ZnSO4 approximately 21fold
PetL expression is positively regulated by the global regulator Fis and negatively regulated by an Hfq-dependent small RNA
-
PetL expression is positively regulated by the global regulator Fis and negatively regulated by an Hfq-dependent small RNA
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
EptA remains active despite encapsulation within a nanostructured bicontinuous cubic phase and displays full transfer of the phosphoethanolamine group from a 1,2-dioleoyl-glycero-phosphoethanolamine doped lipid to monoolein, which makes up the bicontinuous cubic phase
synthesis
-
EptA remains active despite encapsulation within a nanostructured bicontinuous cubic phase and displays full transfer of the phosphoethanolamine group from a 1,2-dioleoyl-glycero-phosphoethanolamine doped lipid to monoolein, which makes up the bicontinuous cubic phase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Herrera, C.M.; Hankins, J.V.; Trent, M.S.
Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides
Mol. Microbiol.
76
1444-1460
2010
Escherichia coli (P30845), Salmonella enterica (P36555), Salmonella enterica LT2 (P36555)
brenda
Anandan, A.; Piek, S.; Kahler, C.; Vrielink, A.
Cloning, expression, purification and crystallization of an endotoxin-biosynthesis enzyme from Neisseria meningitidis
Acta Crystallogr. Sect. F
68
1494-1497
2012
Neisseria meningitidis (Q7DDQ9), Neisseria meningitidis, Neisseria meningitidis NMB (Q7DDQ9)
brenda
Beceiro, A.; Llobet, E.; Aranda, J.; Bengoechea, J.A.; Doumith, M.; Hornsey, M.; Dhanji, H.; Chart, H.; Bou, G.; Livermore, D.M.; Woodford, N.
Phosphoethanolamine modification of lipid A in colistin-resistant variants of Acinetobacter baumannii mediated by the pmrAB two-component regulatory system
Antimicrob. Agents Chemother.
55
3370-3379
2011
Acinetobacter baumannii (E2FGC2)
brenda
Handing, J.W.; Criss, A.K.
The lipooligosaccharide-modifying enzyme LptA enhances gonococcal defence against human neutrophils
Cell. Microbiol.
17
910-921
2015
Neisseria gonorrhoeae (Q5F6F3), Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090 (Q5F6F3)
brenda
Takahashi, H.; Carlson, R.W.; Muszynski, A.; Choudhury, B.; Kim, K.S.; Stephens, D.S.; Watanabe, H.
Modification of lipooligosaccharide with phosphoethanolamine by LptA in Neisseria meningitidis enhances meningococcal adhesion to human endothelial and epithelial cells
Infect. Immun.
76
5777-5789
2008
Neisseria meningitidis (X5ELY0), Neisseria meningitidis
brenda
Lewis, L.A.; Choudhury, B.; Balthazar, J.T.; Martin, L.E.; Ram, S.; Rice, P.A.; Stephens, D.S.; Carlson, R.; Shafer, W.M.
Phosphoethanolamine substitution of lipid A and resistance of Neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serum
Infect. Immun.
77
1112-1120
2009
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA19
brenda
Lewis, L.A.; Shafer, W.M.; Dutta Ray, T.; Ram, S.; Rice, P.A.
Phosphoethanolamine residues on the lipid A moiety of Neisseria gonorrhoeae lipooligosaccharide modulate binding of complement inhibitors and resistance to complement killing
Infect. Immun.
81
33-42
2013
Neisseria gonorrhoeae
brenda
Cullen, T.W.; O'Brien, O.P.; Hendrixson, D.R.; Giles, D.K.; Hobb, R.I.; Thompson, S.A.; Brodbelt, J.S.; Trent, M.S.
EptC of Campylobacter jejuni mediates phenotypes involved in host interactions and virulence
Infect. Immun.
81
430-4440
2013
Campylobacter jejuni (A0A3X8T8A0), Campylobacter jejuni 81-176 (A0A3X8T8A0)
brenda
Cox, A.D.; Wright, J.C.; Li, J.; Hood, D.W.; Moxon, E.R.; Richards, J.C.
Phosphorylation of the lipid A region of meningococcal lipopolysaccharide: identification of a family of transferases that add phosphoethanolamine to lipopolysaccharide
J. Bacteriol.
185
3270-3277
2003
Neisseria meningitidis (X5ELY0), Neisseria meningitidis
brenda
Lee, H.; Hsu, F.F.; Turk, J.; Groisman, E.A.
The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica
J. Bacteriol.
186
4124-4133
2004
Salmonella enterica (Q8Z1P4)
brenda
Tamayo, R.; Choudhury, B.; Septer, A.; Merighi, M.; Carlson, R.; Gunn, J.S.
Identification of cptA, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide core
J. Bacteriol.
187
3391-3399
2005
Salmonella enterica (P36555), Salmonella enterica (Q8Z1P4), Salmonella enterica LT2 (P36555), Salmonella enterica LT2 (Q8Z1P4)
brenda
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
J. Biol. Chem.
276
43111-43121
2001
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 14028
brenda
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
brenda
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
2005
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium C5
brenda
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
J. Biol. Chem.
287
326-3336
2012
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
J. Biol. Chem.
287
38778-38789
2012
Salmonella enterica (Q8Z1P4), Salmonella enterica 14028s (Q8Z1P4)
brenda
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
J. Mol. Biol.
425
3389-3402
2013
Neisseria meningitidis (Q7DD94), Neisseria meningitidis (Q7DDQ9), Neisseria meningitidis, Neisseria meningitidis NMB (Q7DDQ9)
brenda
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
Mol. Microbiol.
27
1171-1182
1998
Salmonella enterica (Q8Z1P4), Salmonella enterica 14028s (Q8Z1P4)
brenda
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
2015
[Haemophilus] ducreyi, [Haemophilus] ducreyi (Q7VMW0), [Haemophilus] ducreyi ATCC 700724 (Q7VMW0)
brenda
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
107
5160-5165
2010
Campylobacter jejuni (A0A3X8T8A0), Campylobacter jejuni
brenda
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
Infect. Immun.
82
2170-2179
2014
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
brenda
Liu, L.; Li, Y.; Wang, X.; Guo, W.
A phosphoethanolamine transferase specific for the 4'-phosphate residue of Cronobacter sakazakii lipid A
J. Appl. Microbiol.
121
1444-1456
2016
Cronobacter sakazakii (A7MFE0), Cronobacter sakazakii, Cronobacter sakazakii BAA894 (A7MFE0)
brenda
Nowicki, E.M.; OBrien, J.P.; Brodbelt, J.S.; Trent, M.S.
Extracellular zinc induces phosphoethanolamine addition to Pseudomonas aeruginosa lipid A via the ColRS two-component system
Mol. Microbiol.
97
166-178
2015
Pseudomonas aeruginosa (A0A069Q704), Pseudomonas aeruginosa
brenda
Piek, S.; Wang, Z.; Ganguly, J.; Lakey, A.M.; Bartley, S.N.; Mowlaboccus, S.; Anandan, A.; Stubbs, K.A.; Scanlon, M.J.; Vrielink, A.; Azadi, P.; Carlson, R.W.; Kahler, C.M.
The role of oxidoreductases in determining the function of the neisserial lipid A phosphoethanolamine transferase required for resistance to polymyxin
PLoS ONE
9
e106513
2014
Neisseria meningitidis (Q7DDQ9), Neisseria meningitidis, Neisseria meningitidis NMB (Q7DDQ9)
brenda
Fage, C.D.; Brown, D.B.; Boll, J.M.; Keatinge-Clay, A.T.; Trent, M.S.
Crystallographic study of the phosphoethanolamine transferase EptC required for polymyxin resistance and motility in Campylobacter jejuni
Acta Crystallogr. Sect. D
70
2730-2739
2014
Campylobacter jejuni (A0A3Z8TVG8), Campylobacter jejuni, Campylobacter jejuni 81-176 (A0A3Z8TVG8)
brenda
Bontemps-Gallo, S.; Cogez, V.; Robbe-Masselot, C.; Quintard, K.; Dondeyne, J.; Madec, E.; Lacroix, J.M.
Biosynthesis of osmoregulated periplasmic glucans in Escherichia coli: the phosphoethanolamine transferase is encoded by opgE
BioMed Res. Int.
2013
371429
2013
Escherichia coli (P75785), Escherichia coli
brenda
Knirel, Y.A.; Lan, R.; Senchenkova, S.N.; Wang, J.; Shashkov, A.S.; Wang, Y.; Perepelov, A.V.; Xiong, Y.; Xu, J.; Sun, Q.
O-antigen structure of Shigella flexneri serotype Yv and effect of the lpt-O gene variation on phosphoethanolamine modification of S. flexneri O-antigens
Glycobiology
23
475-485
2013
Shigella flexneri (S4UV19), Shigella flexneri
brenda
Telke, A.A.; Rolain, J.M.
Functional genomics to discover antibiotic resistance genes: the paradigm of resistance to colistin mediated by ethanolamine phosphotransferase in Shewanella algae MARS 14
Int. J. Antimicrob. Agents
46
648-652
2015
Shewanella algae (A0A0H5BY27), Shewanella algae MARS 14 (A0A0H5BY27)
brenda
Hicks, G.; Jia, Z.
Structural basis for the lipopolysaccharide export activity of the bacterial lipopolysaccharide transport system
Int. J. Mol. Sci.
19
E2680
2018
Escherichia coli (P0ADV1)
brenda
Sherman, D.J.; Lazarus, M.B.; Murphy, L.; Liu, C.; Walker, S.; Ruiz, N.; Kahne, D.
Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport
Proc. Natl. Acad. Sci. USA
111
4982-4987
2014
Neisseria meningitidis serogroup B (Q7DDQ9), Neisseria meningitidis serogroup B MC58 (Q7DDQ9)
brenda
Schultz, K.M.; Lundquist, T.J.; Klug, C.S.
Lipopolysaccharide binding to the periplasmic protein LptA
Protein Sci.
26
1517-1523
2017
Escherichia coli (P0ADV1)
brenda
Stogios, P.J.; Cox, G.; Zubyk, H.L.; Evdokimova, E.; Wawrzak, Z.; Wright, G.D.; Savchenko, A.
Substrate recognition by a colistin resistance enzyme from Moraxella catarrhalis
ACS Chem. Biol.
13
1322-1332
2018
Moraxella sp. HMSC061H09 (A0A1E9VP98)
brenda
Stojanoski, V.; Sankaran, B.; Prasad, B.V.V.; Poirel, L.; Nordmann, P.; Palzkill, T.
Structure of the catalytic domain of the colistin resistance enzyme MCR-1
BMC Biol.
14
81
2016
Escherichia coli (A0A0R6L508)
brenda
Harper, M.; Wright, A.; Michael, F.; Li, J.; Lucas, D.; Ford, M.; Adler, B.; Cox, A.; Boyce, J.
Characterization of two novel lipopolysaccharide phosphoethanolamine transferases in Pasteurella multocida and their role in resistance to cathelicidin-2
Infect. Immun.
85
e00557
2017
Pasteurella multocida, Pasteurella multocida X73
brenda
Liu, L.; Li, Y.; Wang, X.; Guo, W.
A phosphoethanolamine transferase specific for the 4-phosphate residue of Cronobacter sakazakii lipid A
J. Appl. Microbiol.
121
1444-1456
2016
Cronobacter sakazakii, Cronobacter sakazakii BAA894
brenda
Sun, J.; Xu, Y.; Gao, R.; Lin, J.; Wei, W.; Srinivas, S.; Li, D.; Yang, R.-S.; Li, X.-P.; Liao, X.-P.; Liu, Y.-H.; Feng, Y.
Deciphering MCR-2 colistin resistance
mBio
8
e00625
2017
Escherichia coli (A0A1C3NEV1)
brenda
Anandan, A.; Evans, G.L.; Condic-Jurkic, K.; OMara, M.L.; John, C.M.; Phillips, N.J.; Jarvis, G.A.; Wills, S.S.; Stubbs, K.A.; Moraes, I.; Kahler, C.M.; Vrielink, A.
Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding
Proc. Natl. Acad. Sci. USA
114
2218-2223
2017
Neisseria meningitidis serogroup B (Q7DD94), Neisseria meningitidis serogroup B MC58 (Q7DD94)
brenda
Jo, S.; Park, H.; Song, W.; Kim, S.; Kim, E.; Yang, Y.; Kim, J.; Kim, B.; Kim, Y.
Structural characterization of phosphoethanolamine-modified lipid A from probiotic Escherichia coli strain Nissle 1917
RSC Adv.
9
19762-19771
2019
Escherichia coli, Escherichia coli Nissle 1917
-
brenda
van t Hag, L.; Anandan, A.; Seabrook, S.A.; Gras, S.L.; Drummond, C.J.; Vrielink, A.; Conn, C.E.
Direct demonstration of lipid phosphorylation in the lipid bilayer of the biomimetic bicontinuous cubic phase using the confined enzyme lipid A phosphoethanolamine transferase
Soft Matter
13
1493-1504
2017
Neisseria meningitidis serogroup B (Q7DD94), Neisseria meningitidis serogroup B MC58 (Q7DD94)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.7.8.43)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
