Identification of the structural proteins of an ATP-driven potassium transport system in Escherichia coli.
The three structural proteins of the ATP-driven Kdp potassium transport system of Escherichia coli [Rhoads, D. B., Waters, F. B. & Epstein, W. (1976) J. Gen. Physiol. 67, 325-341] have been identified and found to be located in the inner membrane. The high-affinity repressible Kdp system in one of four potassium transport systems in E. coli. The Kdp proteins were identified both in growing cells as well as in heavily UV-irradiated cells infected with transducing phages carrying the kdp operon. Although all previously identified ATP-driven transport systems of Gram-negative bacteria have been shown to contain a periplasmic protein component, no evidence was found for such a component or for an outer membrane component of the Kdp system. The molecular weights of the three inner membrane proteins, KdpA, KdpB, and KdpC, were determined to be 47,000, 90,000 and 22,000, respectively.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000648:ultrastructure; D003090:Coliphages; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005796:Genes; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D011188:Potassium / Q000378:metabolism*
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000255:Adenosine Triphosphate; D011188:Potassium