Modular multidomain phosphoryl transfer proteins of bacteria

Curr Opin Struct Biol. 1997 Jun;7(3):407-15. doi: 10.1016/s0959-440x(97)80059-0.


Recent phylogenetic and structural analyses of multidomain phosphoryl transfer proteins of bacteria have revealed that interdomain (but not intradomain) splicing and fusion, as well as domain duplication and deletion, have occurred frequently during evolution. These events have been found to be exceedingly rare in certain other protein families. Domain-shuffling events are illustrated by examples from the superfamilies of phosphoenolpyruvate-dependent sugar phosphotransferase systems, their transcriptional regulatory protein targets of phosphorylation, sensor autokinase/response regulator signal transduction systems, and permeases of the ATP-binding-cassette type.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Evolution, Molecular
  • Membrane Transport Proteins / metabolism
  • Phosphoenolpyruvate Sugar Phosphotransferase System / chemistry
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism*
  • Phosphorylation
  • Phosphotransferases / metabolism*
  • Phylogeny*
  • Protein Conformation
  • Transcription Factors / metabolism


  • Bacterial Proteins
  • Carrier Proteins
  • Membrane Transport Proteins
  • Transcription Factors
  • LevR protein, Bacillus subtilis
  • Phosphotransferases
  • Phosphoenolpyruvate Sugar Phosphotransferase System