ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system.
Two components of the histidine permease in Salmonella typhimurium, the membrane-bound P and M proteins, react with the photoaffinity labeling reagent 8-azido-ATP in isolated membranes. The extent of labeling is decreased by the addition of ATP and somewhat less by addition of GTP, CTP, UTP, and ADP. Cyclic AMP, NAD, FAD, and S-adenosylmethionine have little effect. We propose that one or both of these proteins have a site capable of binding an adenine nucleotide and that, therefore, they may be involved in the energy-coupling step in active transport.
D018528:ATP-Binding Cassette Transporters; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D026923:Amino Acid Transport Systems, Basic; D001426:Bacterial Proteins; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D026901:Membrane Transport Proteins / Q000302:isolation & purification / Q000378:metabolism*; D008954:Models, Biological; D009245:NADH Dehydrogenase / Q000378:metabolism; D012486:Salmonella typhimurium / Q000201:enzymology*
D018528:ATP-Binding Cassette Transporters; D026923:Amino Acid Transport Systems, Basic; D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; C043828:histidine permease, Bacteria; D000255:Adenosine Triphosphate; D009245:NADH Dehydrogenase; D000251:Adenosine Triphosphatases