Mutational analysis of charged residues in the putative KdpB-TM5 domain of the Kdp-ATPase of Escherichia coli.
Bramkamp
Marc
M
Universität Osnabrück, Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, Germany. bramkamp@biologie.uni-osnabrueck.de
Altendorf
Karlheinz
K
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001665:Binding Sites; D027682:Cation Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009876:Operon; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D027682:Cation Transport Proteins; D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D000251:Adenosine Triphosphatases; C058166:potassium translocating Kdp-ATPase, E coli