Bioinformatic analyses of bacterial HPr kinase/phosphorylase homologues

Res Microbiol. 2005 Apr;156(3):443-51. doi: 10.1016/j.resmic.2004.10.010. Epub 2005 Jan 28.

Abstract

HPr kinase/phosphorylases (HprKs) regulate catabolite repression and sugar transport in Gram-positive bacteria by phosphorylating the small phosphotransferase system (PTS) protein HPr on a serine residue. We identified homologues of HprK in currently sequenced genomes and multiply aligned their sequences in order to perform phylogenetic and motif analyses. Seventy-eight homologues from bacteria and one from an archaeon comprise nine phylogenetic clusters. Some homologues come from bacteria whose genomes contain multiple highly divergent paralogues that cluster loosely together. Many of these proteins are truncated or show little or no identifiable similarity outside of the Walker A nucleotide binding domain. HprK homologues were identified in Gram-negative bacteria that appear to lack PTS permeases, suggesting modes of action and substrates that differ from those characterized in Gram-positive bacteria.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins
  • Cluster Analysis
  • Computational Biology
  • Databases as Topic
  • Gram-Negative Bacteria / enzymology*
  • Gram-Negative Bacteria / genetics
  • Gram-Positive Bacteria / enzymology*
  • Gram-Positive Bacteria / genetics
  • Molecular Sequence Data
  • Phosphorylases / genetics*
  • Phosphorylases / metabolism
  • Phylogeny
  • Protein-Serine-Threonine Kinases / genetics*
  • Protein-Serine-Threonine Kinases / metabolism
  • Sequence Alignment

Substances

  • Bacterial Proteins
  • Phosphorylases
  • HPr kinase
  • Protein-Serine-Threonine Kinases