Genomes and Genes
Gene Symbol: kdpB
Description: potassium translocating ATPase, subunit B
Alias: ECK0685, JW0685, kac
Species: Escherichia coli str. K-12 substr. MG1655
- 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...
- 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...
- 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. ..
- 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 ..
- 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 ..
- 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 ..
- 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...
- 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. 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...
- 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. ..
- 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. ..
- 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
- Bramkamp M, Altendorf K. Functional modules of KdpB, the catalytic subunit of the Kdp-ATPase from Escherichia coli. Biochemistry. 2004;43:12289-96 pubmedThe 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)...
- 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. ..
- 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
- 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. ..
- 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...
- 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 ..
- 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 ..
- 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...
- 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. ..
- 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. ..
- Csonka L, Hanson A. Prokaryotic osmoregulation: genetics and physiology. Annu Rev Microbiol. 1991;45:569-606 pubmed
- 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...
- 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...
- 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...
- 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
- 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...
- 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. ..
- 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...