Functional identification of Proteus mirabilis eptC gene encoding a core lipopolysaccharide phosphoethanolamine transferase

Int J Mol Sci. 2014 Apr 21;15(4):6689-702. doi: 10.3390/ijms15046689.

Abstract

By comparison of the Proteus mirabilis HI4320 genome with known lipopolysaccharide (LPS) phosphoethanolamine transferases, three putative candidates (PMI3040, PMI3576, and PMI3104) were identified. One of them, eptC (PMI3104) was able to modify the LPS of two defined non-polar core LPS mutants of Klebsiella pneumoniae that we use as surrogate substrates. Mass spectrometry and nuclear magnetic resonance showed that eptC directs the incorporation of phosphoethanolamine to the O-6 of L-glycero-D-mano-heptose II. The eptC gene is found in all the P. mirabilis strains analyzed in this study. Putative eptC homologues were found for only two additional genera of the Enterobacteriaceae family, Photobacterium and Providencia. The data obtained in this work supports the role of the eptC (PMI3104) product in the transfer of PEtN to the O-6 of L,D-HepII in P. mirabilis strains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / classification
  • Bacterial Proteins / metabolism*
  • Carbohydrate Sequence
  • Ethanolaminephosphotransferase / chemistry
  • Ethanolaminephosphotransferase / classification
  • Ethanolaminephosphotransferase / metabolism*
  • Genome, Bacterial
  • Klebsiella pneumoniae / metabolism
  • Lipopolysaccharides / chemistry
  • Lipopolysaccharides / metabolism
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Phylogeny
  • Proteus mirabilis / enzymology
  • Proteus mirabilis / genetics
  • Sequence Alignment
  • Spectrometry, Mass, Electrospray Ionization

Substances

  • Bacterial Proteins
  • Lipopolysaccharides
  • Ethanolaminephosphotransferase