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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
in the presence of Ca2+, enzyme transfers the phosphatidylethanolamine group. Stoichiometric amounts of diacylglycerol are generated during the transfer to Kdo2-lipid A
enzyme has a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain of Campylobacter jejuni lipooligosaccharide with a phosphoethanolamine residue
membranes from Escherichia coli grown on 5-50 mM CaCl2 contain a phosphoethanolamine transferase that uses the precursor Kdo2-[4*-32P]lipid IVA as an acceptor. Transferase is not present in membranes of Escherichia coli grown with 5 mM MgCl2, BaCl2, or ZnCl2
Hfq-dependent small RNA MgrR negatively regulates expression of EptB. Envelope stress response protein Sigma E has positively regulates EptB. The effects of Sigma E and deletion of MgrR on levels of EptB mRNA are independent, and the same 5' end is found in both cases. Sigma E acts directly at the level of transcription initiation for EptB, from the same start point as Sigma 70. When Sigma E is active, synthesis of EptB transcript may outstrip MgrR-dependent degradation. A second sRNA, ArcZ, also directly and negatively regulates EptB
enzyme has a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain of Campylobacter jejuni lipooligosaccharide with a phosphoethanolamine residue. FlgG is modified with phosphoethanolamine at a single site, Thr75 by EptC and EptC is unable to modify other amino acids (e.g. serine and tyrosine). Defects in motility arise directly from the loss of phosphoethanolamine modification of FlgG
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Hfq-dependent small RNA MgrR negatively regulates expression of EptB. Envelope stress response protein Sigma E has positively regulates EptB. The effects of Sigma E and deletion of MgrR on levels of EptB mRNA are independent, and the same 5? end is found in both cases. Sigma E acts directly at the level of transcription initiation for EptB, from the same start point as Sigma 70. When Sigma E is active, synthesis of EptB transcript may outstrip MgrR-dependent degradation. A second sRNA, ArcZ, also directly and negatively regulates EptB
membranes from Escherichia coli grown on 5-50 mM CaCl2 contain a phosphoethanolamine transferase that uses the precursor Kdo2-[4*-32P]lipid IVA as an acceptor. Transferase is not present in membranes of Escherichia coli grown with 5 mM MgCl2, BaCl2, or ZnCl2
Ca2+-induced phosphoethanolamine transfer to the outer 3-deoxy-D-manno-octulosonic acid moiety of Escherichia coli. A novel membrane enzyme dependent upon phosphatidylethanolamine
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
Cullen, T.; Madsen, J.; Ivanov, P.; Brodbelt, J.; Trent, M.
Characterization of unique modification of flagellar rod protein FlgG by Campylobacter jejuni lipid A phosphoethanolamine transferase, linking bacterial locomotion and antimicrobial peptide resistance
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History
2.7.8.42 Kdo2-lipid A phosphoethanolamine 7''-transferase
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