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    kdpD sensor histidine kinase KdpD [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946744, updated on 3-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Structural insights into the signal transduction mechanism of the K(+)-sensing two-component system KdpDE.

    Structural insights into the signal transduction mechanism of the K(+)-sensing two-component system KdpDE.
    Xie M, Wu M, Han A.

    11/6/2021
    Structure and function of the juxtamembrane GAF domain of potassium biosensor KdpD.

    Structure and function of the juxtamembrane GAF domain of potassium biosensor KdpD.
    Kumar S, Gillilan RE, Yernool DA., Free PMC Article

    02/6/2021
    The SRP signal sequence of KdpD.

    The SRP signal sequence of KdpD.
    Pross E, Kuhn A., Free PMC Article

    10/31/2020
    In this report authors provide evidence that the extracellular K(+) concentration serves as one of the stimuli sensed by KdpD.

    The sensor kinase KdpD of Escherichia coli senses external K+.
    Laermann V, Ćudić E, Kipschull K, Zimmann P, Altendorf K.

    01/4/2014
    The ArcB and QseC transmembrane (TM) domains are both two-helical motifs, whereas the KdpD TM domain comprises a four-helical bundle with shorter second and third helices. The interhelical distances reveal weak interactions of all three receptors.

    Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis.
    Maslennikov I, Klammt C, Hwang E, Kefala G, Okamura M, Esquivies L, Mörs K, Glaubitz C, Kwiatkowski W, Jeon YH, Choe S., Free PMC Article

    07/19/2010
    The response regulator KdpE receives the phosphoryl group from KdpD and induces kdpFABC transcription.

    The complexity of the 'simple' two-component system KdpD/KdpE in Escherichia coli.
    Heermann R, Jung K.

    06/28/2010
    Data 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.

    Influence of K+-dependent membrane lipid composition on the expression of the kdpFABC operon in Escherichia coli.
    Schniederberend M, Zimmann P, Bogdanov M, Dowhan W, Altendorf K., Free PMC Article

    04/12/2010
    The Usp domain within KdpD is important for proper KdpD/KdpE signaling.

    Domain swapping reveals that the N-terminal domain of the sensor kinase KdpD in Escherichia coli is important for signaling.
    Heermann R, Lippert ML, Jung K., Free PMC Article

    01/21/2010
    Dephosphorylated IIANtr enhances activity of the kdp promoter by direct binding of dephosphorylated IIA(Ntr) to the sensor kinase KdpD.

    Stimulation of the potassium sensor KdpD kinase activity by interaction with the phosphotransferase protein IIA(Ntr) in Escherichia coli.
    Lüttmann D, Heermann R, Zimmer B, Hillmann A, Rampp IS, Jung K, Görke B.

    01/21/2010
    The universal stress protein UspC scaffolds the KdpD/KdpE signaling cascade of Escherichia coli under salt stress

    The universal stress protein UspC scaffolds the KdpD/KdpE signaling cascade of Escherichia coli under salt stress.
    Heermann R, Weber A, Mayer B, Ott M, Hauser E, Gabriel G, Pirch T, Jung K.

    01/21/2010
    Data indicate that stimulus perception by KdpD does not correlate with changes in the cytoplasmic volume, in the intracellular ATP or K(+) concentration. Data propose that a reduction in turgor cannot be the stimulus for KdpD.

    Reduction of turgor is not the stimulus for the sensor kinase KdpD of Escherichia coli.
    Hamann K, Zimmann P, Altendorf K., Free PMC Article

    01/21/2010
    These data clearly show that the extension of the fourth transmembrane helix encompassing the arginine cluster is mainly involved in sensing both K+ limitation and osmotic upshift, which may not be separated mechanistically.

    The extension of the fourth transmembrane helix of the sensor kinase KdpD of Escherichia coli is involved in sensing.
    Zimmann P, Steinbrügge A, Schniederberend M, Jung K, Altendorf K., Free PMC Article

    01/21/2010
    the sensing and response functions are both located in the C-terminal domain

    The cytoplasmic C-terminal domain of the Escherichia coli KdpD protein functions as a K+ sensor.
    Rothenbücher MC, Facey SJ, Kiefer D, Kossmann M, Kuhn A., Free PMC Article

    01/21/2010
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