KdpD is a tandem serine histidine kinase that controls K+ pump KdpFABC transcriptionally and post-translationally

Jakob M. Silberberg, Sophie Ketter, Paul J. N. Böhm, Kristin Jordan, Marcel Wittenberg, Julia Grass and Inga Hänelt ()
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Jakob M. Silberberg: Goethe University Frankfurt
Sophie Ketter: Goethe University Frankfurt
Paul J. N. Böhm: Goethe University Frankfurt
Kristin Jordan: Goethe University Frankfurt
Marcel Wittenberg: Goethe University Frankfurt
Julia Grass: Goethe University Frankfurt
Inga Hänelt: Goethe University Frankfurt

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract Two-component systems, consisting of a histidine kinase and a response regulator, serve signal transduction in bacteria, often regulating transcription in response to environmental stimuli. Here, we identify a tandem serine histidine kinase function for KdpD, previously described as a histidine kinase of the KdpDE two-component system, which controls production of the potassium pump KdpFABC. We show that KdpD additionally mediates an inhibitory serine phosphorylation of KdpFABC at high potassium levels, using not its C-terminal histidine kinase domain but an N-terminal atypical serine kinase domain. Sequence analysis of KdpDs from different species highlights that some KdpDs are much shorter than others. We show that, while Escherichia coli KdpD’s atypical serine kinase domain responds directly to potassium levels, a shorter version from Deinococcus geothermalis is controlled by second messenger cyclic di-AMP. Our findings add to the growing functional diversity of sensor kinases while simultaneously expanding the framework for regulatory mechanisms in bacterial potassium homeostasis.

Date: 2024
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DOI: 10.1038/s41467-024-47526-8

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