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

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 dir

SUBMITTER: Silberberg JM 

PROVIDER: S-EPMC11018627 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature