The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins

FEMS Microbiol Lett. 1999 Jul 1;176(1):111-6. doi: 10.1111/j.1574-6968.1999.tb13650.x.


Mutations in the cytoplasmic linker regions of receptor histidine kinase and chemoreceptor proteins have been shown previously to significantly impair receptor functions. Here we demonstrate significant sequence similarities between these regions in numerous histidine kinases, methyl-accepting proteins, adenylyl cyclases and other prokaryotic signalling proteins. It is suggested that these 'HAMP domains' possess roles of regulating the phosphorylation or methylation of homodimeric receptors by transmitting the conformational changes in periplasmic ligand-binding domains to cytoplasmic signalling kinase and methyl-acceptor domains.

MeSH terms

  • Adenylyl Cyclases / genetics
  • Amino Acid Sequence
  • Bacteria / chemistry
  • Bacteria / enzymology
  • Bacteria / genetics*
  • Genes, Bacterial*
  • Histidine Kinase
  • Molecular Sequence Data
  • Phosphoric Monoester Hydrolases / genetics
  • Protein Kinases / genetics*
  • Proteins / genetics*
  • Receptors, Cytoplasmic and Nuclear / genetics*
  • Receptors, Peptide / genetics
  • Sequence Alignment


  • MeAP29 protein, rat
  • Proteins
  • Receptors, Cytoplasmic and Nuclear
  • Receptors, Peptide
  • Protein Kinases
  • Histidine Kinase
  • Phosphoric Monoester Hydrolases
  • Adenylyl Cyclases