Genomes and Genes
Gene Symbol: kdpC
Description: potassium translocating ATPase, subunit C
Alias: ECK0684, JW0684, kac
Species: Escherichia coli str. K-12 substr. MG1655
- Csonka L, Hanson A. Prokaryotic osmoregulation: genetics and physiology. Annu Rev Microbiol. 1991;45:569-606 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. ..
- 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. ..
- Ahnert F, Schmid R, Altendorf K, Greie J. ATP binding properties of the soluble part of the KdpC subunit from the Escherichia coli K(+)-transporting KdpFABC P-type ATPase. Biochemistry. 2006;45:11038-46 pubmed..the catalytic P-type ATPase subunit, but ATP binding also occurs in the essential but noncatalytic subunit, KdpC. For further characterization, the soluble portion of KdpC (KdpC(sol), residues Asn39-Glu190) was synthesized ..
- Nakashima K, Sugiura A, Kanamaru K, Mizuno T. Signal transduction between the two regulatory components involved in the regulation of the kdpABC operon in Escherichia coli: phosphorylation-dependent functioning of the positive regulator, KdpE. Mol Microbiol. 1993;7:109-16 pubmed
- Hu G, Rice W, Dröse S, Altendorf K, Stokes D. Three-dimensional structure of the KdpFABC complex of Escherichia coli by electron tomography of two-dimensional crystals. J Struct Biol. 2008;161:411-8 pubmed..These results illustrate the utility of electron tomography in structure determination of ordered assemblies, especially when disorder is severe enough to hamper conventional crystallographic analysis. ..
- 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..KdpF, could be identified on high resolution SDS-polyacrylamide gels in addition to the subunits KdpA, KdpB, and KdpC. Furthermore, it could be demonstrated that KdpF remains associated with the purified complex...
- 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. ..
- Altendorf K, Gassel M, Puppe W, Möllenkamp T, Zeeck A, Boddien C, et al. Structure and function of the Kdp-ATPase of Escherichia coli. Acta Physiol Scand Suppl. 1998;643:137-46 pubmedThe kdpFABC operon of Escherichia coli consists of the four structural genes kdpF, kdpA, kdpB, and kdpC. Expression of the kdpF gene was demonstrated using minicells of E. coli...
- Buurman E, Kim K, Epstein W. Genetic evidence for two sequentially occupied K+ binding sites in the Kdp transport ATPase. J Biol Chem. 1995;270:6678-85 pubmed..Energy coupling in Kdp, mediated by the KdpB subunit, is performed by a different subunit from the one that mediates transport. ..
- Sugiura A, Nakashima K, Tanaka K, Mizuno T. Clarification of the structural and functional features of the osmoregulated kdp operon of Escherichia coli. Mol Microbiol. 1992;6:1769-76 pubmed..e. in addition to them, a cis-acting sequence located upstream of the -35 region was essential for full activation of the promoter. This upstream sequence was demonstrated to be the target site for the trans-acting activator, KdpE. ..
- Sardesai A, Gowrishankar J. Improvement in K+-limited growth rate associated with expression of the N-terminal fragment of one subunit (KdpA) of the multisubunit Kdp transporter in Escherichia coli. J Bacteriol. 2001;183:3515-20 pubmed..able to mediate an improvement in K+-limited growth rates in two different contexts, even in the absence of both KdpC and the ATPase subunit KdpB...
- 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..The cytosolic C-terminal domain of the KdpC subunit, which is assumed to play a role in cooperative ATP binding together with KdpB, is located in close ..
- Irzik K, Pfrötzschner J, Goss T, Ahnert F, Haupt M, Greie J. The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone. FEBS J. 2011;278:3041-53 pubmed publisher..blending of these two groups of transporters in KdpFABC also entails a nucleotide-binding mechanism in which the KdpC subunit acts as a catalytic chaperone...
- 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. ..
- Stumpe -, Bakker -. Requirement of a large K+-uptake capacity and of extracytoplasmic protease activity for protamine resistance of Escherichia coli. Arch Microbiol. 1997;167:126-36 pubmed..Cells that cannot take up K+ rapidly remain metabolically compromised to such an extent that extracytoplasmic protease activity is not induced, leading to a prolonged susceptibility of the cells to the toxic peptide. ..
- Trchounian A. Ion exchange in facultative anaerobes: does a proton-potassium pump exist in anaerobic Escherichia Coli?. Anaerobe. 1997;3:355-71 pubmed
- 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. ..
- 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..Subunit KdpC has long been thought to exhibit an FXYD protein-like function in the regulation of KdpFABC activity...
- 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
- Epstein W, Davies M. Potassium-dependant mutants of Escherichia coli K-12. J Bacteriol. 1970;101:836-43 pubmed..1 mm. The mutants do not appear to have a primary alteration in K transport, and are therefore referred to as K-dependent. The abbreviation kdp is proposed for this class of mutant. ..
- Altendorf K, Siebers A, Epstein W. The KDP ATPase of Escherichia coli. Ann N Y Acad Sci. 1992;671:228-43 pubmed