ATP-dependent protein kinases in bacteria.
Protein phosphorylation has been shown to occur in over fifty different bacterial species and, therefore, seems to be a universal device among prokaryotes. Most of the protein kinases responsible for this modification of proteins share the common property of using adenosine triphosphate as phosphoryl donor. However, they differ from one another in a number of structural and functional aspects. Namely, they exhibit a varying acceptor amino acid specificity and can be classified, on this basis, in three main groups: protein-histidine kinases, protein-serine/threonine kinases and protein-tyrosine kinases.
Cozzone
A J
AJ
Institut de Biologie et Chimie des Protéines, Centre National de la Recherche Scientifique, Lyon, France.
D000255:Adenosine Triphosphate / Q000502:physiology*; D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism*; D000071677:Histidine Kinase; D010766:Phosphorylation; D011494:Protein Kinases / Q000145:classification / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D015398:Signal Transduction
D001426:Bacterial Proteins; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D000071677:Histidine Kinase