kdpB

Summary

Gene Symbol: kdpB
Description: potassium translocating ATPase, subunit B
Alias: ECK0685, JW0685, kac
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Schniederberend M, Zimmann P, Bogdanov M, Dowhan W, Altendorf K. Influence of K+-dependent membrane lipid composition on the expression of the kdpFABC operon in Escherichia coli. Biochim Biophys Acta. 2010;1798:32-9 pubmed publisher
    ..Finally, we show that kinase activity of KdpD is stimulated in its native membrane environment by fusion with liposomes of anionic, but reduced with liposomes of zwitterionic phospholipids. ..
  2. 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
    ..composition and is notable for segregating K+ transport and ATP hydrolysis onto separate subunits (KdpA and KdpB, respectively)...
  3. 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
    ..In the K(+)-transporting KdpFABC complex of Escherichia coli, KdpB resembles the catalytic P-type ATPase subunit, but ATP binding also occurs in the essential but noncatalytic ..
  4. 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. ..
  5. Bramkamp M, Altendorf K. Mutational analysis of charged residues in the putative KdpB-TM5 domain of the Kdp-ATPase of Escherichia coli. Ann N Y Acad Sci. 2003;986:351-3 pubmed
  6. 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.
  7. 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
    ..polypeptide, 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...
  8. Damnjanović B, Weber A, Potschies M, Greie J, Apell H. Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase. Biochemistry. 2013;52:5563-76 pubmed publisher
  9. 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
    ..of Escherichia coli, which belongs to the P-type ATPase family, has a unique structure, since catalytic activity (KdpB) and the capacity to transport potassium ions (KdpA) are located on different subunits...

More Information

Publications40

  1. 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 pubmed
    The 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...
  2. 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
    ..On the basis of the biochemical properties of the ATP-hydrolyzing subunit KdpB, the transport complex is classified as type IA P-type ATPase...
  3. 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. ..
  4. 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 K+-translocating KdpA subunit is in close contact with the transmembrane region of the ATP-hydrolyzing subunit KdpB. The cytosolic C-terminal domain of the KdpC subunit, which is assumed to play a role in cooperative ATP binding ..
  5. 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
    ..in K+-limited growth rates in two different contexts, even in the absence of both KdpC and the ATPase subunit KdpB. The first context was when KdpA' was overexpressed in cells from a heterologous inducible promoter, and the second ..
  6. Heitkamp T, Kalinowski R, Bottcher B, Börsch M, Altendorf K, Greie J. K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer. Biochemistry. 2008;47:3564-75 pubmed publisher
    ..In the present work, a close vicinity of two KdpB subunits within the functional KdpFABC complex could be demonstrated by chemical cross-linking of native cysteine ..
  7. 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
    ..All typical features of P-type ATPases are attributed to the KdpB subunit, which also comprises strong structural homologies to other P-type ATPase family members...
  8. Trchounian A. Ion exchange in facultative anaerobes: does a proton-potassium pump exist in anaerobic Escherichia Coli?. Anaerobe. 1997;3:355-71 pubmed
  9. 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
    ..mutagenesis of the charged residues aspartate 583 and lysine 586 in the putative transmembrane helix V of subunit KdpB revealed that these charges are involved in the coupling of ATP hydrolysis and ion translocation...
  10. 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. ..
  11. 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. ..
  12. 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. ..
  13. Altendorf K, Siebers A, Epstein W. The KDP ATPase of Escherichia coli. Ann N Y Acad Sci. 1992;671:228-43 pubmed
  14. Bramkamp M, Altendorf K. Functional modules of KdpB, the catalytic subunit of the Kdp-ATPase from Escherichia coli. Biochemistry. 2004;43:12289-96 pubmed
    The large cytoplasmic domain (H4H5) of KdpB of the KdpFABC complex (P-type ATPase) from Escherichia coli consists of two separate modules, the phosphorylation domain (KdpBP) and the nucleotide binding domain (KdpBN)...
  15. Asha H, Gowrishankar J. Regulation of kdp operon expression in Escherichia coli: evidence against turgor as signal for transcriptional control. J Bacteriol. 1993;175:4528-37 pubmed
    ..On the basis of these data, we discuss alternative candidates that might serve as the signal for control of kdp operon transcription. ..
  16. Haupt M, Coles M, Truffault V, Bramkamp M, Altendorf K, Kessler H. 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli. J Biomol NMR. 2004;29:437-8 pubmed
  17. Ohashi K, Yamashino T, Mizuno T. Molecular basis for promoter selectivity of the transcriptional activator OmpR of Escherichia coli: isolation of mutants that can activate the non-cognate kdpABC promoter. J Biochem. 2005;137:51-9 pubmed
    ..We propose that the promoter selectivity of OmpR is determined not only by its DNA-binding specificity, but also by the spatial configuration of the promoter on which OmpR must properly associate with RNA polymerase. ..
  18. 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...
  19. Hesse J, Wieczorek L, Altendorf K, Reicin A, Dorus E, Epstein W. Sequence homology between two membrane transport ATPases, the Kdp-ATPase of Escherichia coli and the Ca2+-ATPase of sarcoplasmic reticulum. Proc Natl Acad Sci U S A. 1984;81:4746-50 pubmed
    ..Regions of the predicted amino acid sequence of KdpB, the phosphorylated protein of the system, are homologous to regions of the Ca2+-ATPase of rabbit sarcoplasmic ..
  20. Haupt M, Bramkamp M, Heller M, Coles M, Deckers Hebestreit G, Herkenhoff Hesselmann B, et al. The holo-form of the nucleotide binding domain of the KdpFABC complex from Escherichia coli reveals a new binding mode. J Biol Chem. 2006;281:9641-9 pubmed
    ..The KdpB subunit of the prokaryotic Kdp-ATPase (KdpFABC complex) shares characteristic regions of homology with class II-IV ..
  21. 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
    ..high affinity ATP-driven K+-transport system of Escherichia coli, is a complex of the membrane-bound subunits KdpA, KdpB, KdpC and the small peptide KdpF...
  22. Stumpe S, Bakker E. 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. ..
  23. Nakashima K, Sugiura A, Momoi H, Mizuno T. Phosphotransfer signal transduction between two regulatory factors involved in the osmoregulated kdp operon in Escherichia coli. Mol Microbiol. 1992;6:1777-84 pubmed
    ..We also developed a procedure for preparing cytoplasmic membrane enriched with the KdpD protein that exhibits in vitro ability with regard to phosphorylation of KdpE protein. ..
  24. Csonka L, Hanson A. Prokaryotic osmoregulation: genetics and physiology. Annu Rev Microbiol. 1991;45:569-606 pubmed
  25. Puppe W, Siebers A, Altendorf K. The phosphorylation site of the Kdp-ATPase of Escherichia coli: site-directed mutagenesis of the aspartic acid residues 300 and 307 of the KdpB subunit. Mol Microbiol. 1992;6:3511-20 pubmed
    ..The KdpB subunit has been identified as the catalytic subunit forming the phosphorylated intermediate...
  26. 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...
  27. Gassel M, Altendorf K. Analysis of KdpC of the K(+)-transporting KdpFABC complex of Escherichia coli. Eur J Biochem. 2001;268:1772-81 pubmed
    ..ATP-driven K(+) transport system of Escherichia coli, is composed of the four membrane-bound subunits KdpF, KdpA, KdpB and KdpC...
  28. 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
  29. Becker D, Fendler K, Altendorf K, Greie J. The conserved dipole in transmembrane helix 5 of KdpB in the Escherichia coli KdpFABC P-type ATPase is crucial for coupling and the electrogenic K+-translocation step. Biochemistry. 2007;46:13920-8 pubmed
    ..charged residues, D583 and K586, which are located at the center of transmembrane helix 5 (TM 5) of the catalytic KdpB subunit, and which are supposed to establish a dipole involved in energy coupling...
  30. 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. ..
  31. Haupt M, Bramkamp M, Coles M, Altendorf K, Kessler H. Inter-domain motions of the N-domain of the KdpFABC complex, a P-type ATPase, are not driven by ATP-induced conformational changes. J Mol Biol. 2004;342:1547-58 pubmed
    ..Here, we present the solution structure of the nucleotide binding domain of KdpB (backbone RMSD 0.17 A) and a model of the AMP-PNP binding mode based on intermolecular distance restraints...