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Gene Review:

lpxA - UDP-N-acetylglucosamine acetyltransferase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0180, JW0176

Dotson, G.D. et al., Kelly, T.M. et al., Crowell, D.N. et al., Klena, J.D. et al., Sweet, C.R. et al., et al.

Klena, Parker, Knibb, Ibbitt, Devane, Horn, Miller, Konkel,

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Disease relevance of lpxA

Molecular cloning of the genes for lipid A disaccharide synthase and UDP-N-acetylglucosamine acyltransferase in Escherichia coli [1].
We now demonstrate that the lpxA gene from Neisseria meningitidis encodes a similar acyltransferase that selectively utilizes 3-hydroxylauroyl-ACP [2].
We here report the isolation of the lpxA gene of Pseudomonas aeruginosa from a library of Pseudomonas strain PAO1 expressed in Escherichia coli LE392 (J. Lightfoot and J. S. Lam, J. Bacteriol. 173:5624-5630, 1991) [3].
Differentiation of Campylobacter coli, Campylobacter jejuni, Campylobacter lari, and Campylobacter upsaliensis by a multiplex PCR developed from the nucleotide sequence of the lipid A gene lpxA [4].
A Chlamydia trachomatis UDP-N-acetylglucosamine acyltransferase selective for myristoyl-acyl carrier protein. Expression in Escherichia coli and formation of hybrid lipid A species [5].

High impact information on lpxA

The genes encoding these proteins were recognized because of their location between lpxA and lpxB in A. ferrooxidans [6].
The possibility that the firA gene of Escherichia coli (Dicker, I. B., and Seetharam, S. (1991) Mol. Microbiol. 6, 817-823) might function in lipid A biosynthesis was examined based on its homology to the lpxA gene, which encodes UDP-N-acetylglucosamine O-acyl-transferase, the first enzyme in lipid A formation [7].
Sequencing revealed that it contains one complete open reading frame (777 bp) encoding a new lpxA homolog [3].
Pseudomonas lpxA encodes a 10-carbon-specific UDP-GlcNAc acyltransferase, whereas the E. coli transferase is selective for a 14-carbon acyl chain [3].
Cloning and sequence analysis of chromosomal DNA downstream of lpxD revealed the presence of the fabZ and lpxA genes [8].

Chemical compound and disease context of lpxA

Crystals of UDP-N-acetylglucosamine O-acyltransferase (lpxA) from Escherichia coli have been obtained from solutions of sodium/potassium phosphate and dimethylsulfoxide [9].

Biological context of lpxA

The 5'-end of the B. burgdorferi lon gene appears to suppress the temperature-sensitive phenotype of an E. coli lpxA mutant [10].
A mutation of lpxA, functioning at the first stage in lipid A biosynthesis, inhibited both cell division and growth, producing short filaments [11].

Other interactions of lpxA

Two of these are lipid A disaccharide synthase and UDP-N-acetylglucosamine acyltransferase [1].

References

Molecular cloning of the genes for lipid A disaccharide synthase and UDP-N-acetylglucosamine acyltransferase in Escherichia coli. Crowell, D.N., Anderson, M.S., Raetz, C.R. J. Bacteriol. (1986) [Pubmed]
Shortened hydroxyacyl chains on lipid A of Escherichia coli cells expressing a foreign UDP-N-acetylglucosamine O-acyltransferase. Odegaard, T.J., Kaltashov, I.A., Cotter, R.J., Steeghs, L., van der Ley, P., Khan, S., Maskell, D.J., Raetz, C.R. J. Biol. Chem. (1997) [Pubmed]
Expression cloning of a Pseudomonas gene encoding a hydroxydecanoyl-acyl carrier protein-dependent UDP-GlcNAc acyltransferase. Dotson, G.D., Kaltashov, I.A., Cotter, R.J., Raetz, C.R. J. Bacteriol. (1998) [Pubmed]
Differentiation of Campylobacter coli, Campylobacter jejuni, Campylobacter lari, and Campylobacter upsaliensis by a multiplex PCR developed from the nucleotide sequence of the lipid A gene lpxA. Klena, J.D., Parker, C.T., Knibb, K., Ibbitt, J.C., Devane, P.M., Horn, S.T., Miller, W.G., Konkel, M.E. J. Clin. Microbiol. (2004) [Pubmed]
A Chlamydia trachomatis UDP-N-acetylglucosamine acyltransferase selective for myristoyl-acyl carrier protein. Expression in Escherichia coli and formation of hybrid lipid A species. Sweet, C.R., Lin, S., Cotter, R.J., Raetz, C.R. J. Biol. Chem. (2001) [Pubmed]
Oxidation and transamination of the 3"-position of UDP-N-acetylglucosamine by enzymes from Acidithiobacillus ferrooxidans. Role in the formation of lipid a molecules with four amide-linked acyl chains. Sweet, C.R., Ribeiro, A.A., Raetz, C.R. J. Biol. Chem. (2004) [Pubmed]
The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis. Kelly, T.M., Stachula, S.A., Raetz, C.R., Anderson, M.S. J. Biol. Chem. (1993) [Pubmed]
Isolation and characterization of the Neisseria meningitidis lpxD-fabZ-lpxA gene cluster involved in lipid A biosynthesis. Steeghs, L., Jennings, M.P., Poolman, J.T., van der Ley, P. Gene (1997) [Pubmed]
Crystallization of UDP-N-acetylglucosamine O-acyltransferase from Escherichia coli. Pfitzner, U., Raetz, C.R., Roderick, S.L. Proteins (1995) [Pubmed]
Cloning and expression of the Borrelia burgdorferi lon gene. Cloud, J.L., Marconi, R.T., Eggers, C.H., Garon, C.F., Tilly, K., Samuels, D.S. Gene (1997) [Pubmed]
kdsA mutations affect FtsZ-ring formation in Escherichia coli K-12. Fujishima, H., Nishimura, A., Wachi, M., Takagi, H., Hirasawa, T., Teraoka, H., Nishimori, K., Kawabata, T., Nishikawa, K., Nagai, K. Microbiology (Reading, Engl.) (2002) [Pubmed]

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