Literature summary for 2.3.1.191 extracted from

Vuorio, R.; H�rk�nen, T.; Tolvanen, M.; Vaara, M.
The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of lipid A biosynthesis is conserved in various bacteria (1994), FEBS Lett., 337, 289-292.

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Organism

Organism	UniProt	Comment	Textmining
Yersinia enterocolitica	P32203	about half of the LpxD protein is made of hexad repeats (26 repeating hexapeptides). The lpxD gene from Yersinia enterocolitica is sequenced and the deduced amino acid sequence is compared with the lpxD sequences of Escherichia coli and Salmonella typhimurium. The hexapeptide repeat pattern is a very conservative property of these enzymes. Even though the overall homology between the proteins is 58%, the homology in the first residue of each hexapeptide is 100%	-

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Release 2023.1 (January 2023)