A proposed link between nitrogen and carbon metabolism involving protein phosphorylation in bacteria

Protein Sci. 1992 Jun;1(6):722-6. doi: 10.1002/pro.5560010604.

Abstract

We demonstrate that certain phosphoryl transfer proteins of the bacterial phosphotransferase system (PTS), the fructose- and mannitol-specific IIA proteins or domains, are homologous to a class of proteins, one of which is known to affect transcription of some of the nitrogen-regulatory sigma 54-dependent operons in Klebsiella pneumoniae. The phosphorylatable histidyl residue in the homologous PTS proteins and the consensus sequence in the vicinity of the active-site histidine are fully conserved in all members that comprise this family of proteins. A phylogenetic tree of the eight protein members of this family was constructed, and a "signature" sequence that can serve for the identification of new protein members of this family is proposed. These observations suggest that PTS-catalyzed protein phosphorylation may provide a regulatory link between carbon and nitrogen assimilation in bacteria.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Bacteria / enzymology*
  • Bacteria / genetics
  • Carbon / metabolism*
  • Fructose / metabolism
  • Klebsiella pneumoniae / enzymology*
  • Klebsiella pneumoniae / genetics
  • Mannitol / metabolism
  • Molecular Sequence Data
  • Nitrogen / metabolism*
  • Open Reading Frames
  • Operon
  • Phosphoenolpyruvate Sugar Phosphotransferase System / genetics
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism*
  • Phosphorylation
  • Phylogeny
  • Sequence Homology, Amino Acid
  • Sigma Factor / metabolism
  • Transcription, Genetic

Substances

  • Sigma Factor
  • Fructose
  • Mannitol
  • Carbon
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • Nitrogen