The role of phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, in the regulation of carbon metabolism in gram-positive bacteria.
HPr of the Gram-positive bacterial phosphotransferase system (PTS) can be phosphorylated by an ATP-dependent protein kinase on a serine residue or by PEP-dependent Enzyme 1 on a histidyl residue. Both phosphorylation events appear to influence the metabolism of non-PTS carbon sources. Catabolite repression of the gluconate (gnt) operon of B. subtilis appears to be regulated by the former phosphorylation event, while glycerol kinase appears to be regulated by the latter phosphorylation reaction. The extent of our understanding of these processes will be described.
Reizer
J
J
Department of Biology, University of California, San Diego, La Jolla 92093-0116.
Romano
A H
AH
Deutscher
J
J
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D002244:Carbon / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D006094:Gram-Positive Bacteria / Q000378:metabolism*; D006639:Histidine / Q000378:metabolism; D000071677:Histidine Kinase; D008969:Molecular Sequence Data; D009876:Operon; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000378:metabolism; D013045:Species Specificity
D001426:Bacterial Proteins; D012694:Serine; D006639:Histidine; D002244:Carbon; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; D017346:Protein Serine-Threonine Kinases; D000071677:Histidine Kinase