Gene Symbol: kdpF
Description: potassium ion accessory transporter subunit
Alias: ECK0687, JW0687
Species: Escherichia coli str. K-12 substr. MG1655
- Bramkamp M, Gassel M, Altendorf K. FITC binding site and p-nitrophenyl phosphatase activity of the Kdp-ATPase of Escherichia coli. Biochemistry. 2004;43:4559-67 pubmed..The notion that FITC inhibits pNPPase and ATPase activity supports the idea that the catalytic domain of KdpB is much more compact than other P-type ATPases, like Na(+),K(+)-ATPase, H(+),K(+)-ATPase, and Ca(2+)-ATPase. ..
- Greie J, Altendorf K. The K+-translocating KdpFABC complex from Escherichia coli: a P-type ATPase with unique features. J Bioenerg Biomembr. 2007;39:397-402 pubmed
- Siebers A, Altendorf K. Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli. J Biol Chem. 1989;264:5831-8 pubmed..The KdpB polypeptide was identified as the phosphorylated subunit after electrophoretic separation at pH 2.4, 4 degrees C of cytoplasmic membranes or of purified ATPase labeled with [gamma-32P]ATP. ..
- Gassel M, Altendorf K. Analysis of KdpC of the K(+)-transporting KdpFABC complex of Escherichia coli. Eur J Biochem. 2001;268:1772-81 pubmed..high affinity ATP-driven K(+) transport system of Escherichia coli, is composed of the four membrane-bound subunits KdpF, KdpA, KdpB and KdpC...
- Bertrand J, Altendorf K, Bramkamp M. Amino acid substitutions in putative selectivity filter regions III and IV in KdpA alter ion selectivity of the KdpFABC complex from Escherichia coli. J Bacteriol. 2004;186:5519-22 pubmed..Replacement of the glycine residues in KdpA at positions 345 and 470, members of putative selectivity filter regions III and IV, alters the ion selectivity of the KdpFABC complex. ..
- Bramkamp M, Altendorf K. Single amino acid substitution in the putative transmembrane helix V in KdpB of the KdpFABC complex of Escherichia coli uncouples ATPase activity and ion transport. Biochemistry. 2005;44:8260-6 pubmed
- Gassel M, Siebers A, Epstein W, Altendorf K. Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli. Biochim Biophys Acta. 1998;1415:77-84 pubmed..system of Escherichia coli, is a complex of the membrane-bound subunits KdpA, KdpB, KdpC and the small peptide KdpF. The assembly of this complex was studied by the analysis of mutants that expressed two of the three large subunits ..
- Siebers A, Altendorf K. The K+-translocating Kdp-ATPase from Escherichia coli. Purification, enzymatic properties and production of complex- and subunit-specific antisera. Eur J Biochem. 1988;178:131-40 pubmed..In functional inhibition studies the anti-KdpABC and anti-KdpB sera impaired ATPase activity in the membrane-bound as well as in the purified state of the enzyme. In contrast, the anti-KdpC serum did not inhibit enzyme activity. ..
- Trchounian A. Ion exchange in facultative anaerobes: does a proton-potassium pump exist in anaerobic Escherichia Coli?. Anaerobe. 1997;3:355-71 pubmed
- Rhoads D, Laimins L, Epstein W. Functional organization of the kdp genes of Escherichia coli K-12. J Bacteriol. 1978;135:445-52 pubmed..Deletions extending clockwise from kdp as far as the gltA locus were isolated from strains with bacteriophage lambda integrated into kdpD. Plaque-forming transducing lambda phages carrying the kdpABC operon were isolated. ..
- Gassel M, Möllenkamp T, Puppe W, Altendorf K. The KdpF subunit is part of the K(+)-translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro. J Biol Chem. 1999;274:37901-7 pubmed..Upon expression of this operon in minicells, a so far unrecognized small hydrophobic polypeptide, KdpF, could be identified on high resolution SDS-polyacrylamide gels in addition to the subunits KdpA, KdpB, and KdpC...
- Bramkamp M, Altendorf K, Greie J. Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex from Escherichia coli (Review). Mol Membr Biol. 2007;24:375-86 pubmed..This review compares generic features of P-type ATPases with the rather unique KdpFABC complex and gives a comprehensive overview of common principles of catalysis as well as of special aspects connected to distinct enzyme functions. ..
- Heitkamp T, Bottcher B, Greie J. Solution structure of the KdpFABC P-type ATPase from Escherichia coli by electron microscopic single particle analysis. J Struct Biol. 2009;166:295-302 pubmed publisher..Overall, the arrangement of subunits agrees with biochemical data and the predictions on subunit interactions. ..