Literature summary for 2.7.8.42 extracted from

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 (2012), J. Biol. Chem., 287, 3326-3336.

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Organism

Organism	UniProt	Comment	Textmining
Campylobacter jejuni	-	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	-

Synonyms

Synonyms	Comment	Organism
lipid A phosphoethanolamine transferase	-	Campylobacter jejuni

General Information

General Information	Comment	Organism
physiological function	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	Campylobacter jejuni

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Release 2023.1 (January 2023)