title: Diversity and specificity of protein-phosphorylating systems in bacteria.
abstract: Bacteria harbor three different protein-phosphorylating systems which regulate distinct physiological processes: first, the nucleotide-dependent system which modifies hydroxyl groups of amino acids in protein substrates; second, the two-component system which involves both sensor kinase and response regulator; third, the phosphoenolpyruvate-dependent phosphotransferase system. These systems share a number of structural and functional similarities with the protein-phosphorylating systems of eukaryotes.
authors.affiliation: Institut de Biologie et Chimie des Protéines, CNRS, Lyon, France.
authors.forename: A J
authors.initials: AJ
authors.lastname: Cozzone
mesh_terms: D000220:Adaptation, Biological; D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000378:metabolism; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism; D010766:Phosphorylation; D011387:Prokaryotic Cells / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D011494:Protein Kinases; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; D011505:Protein-Tyrosine Kinases