ArticleFEBS letters2020
Escherichia coli YegI is a novel Ser/Thr kinase lacking conserved motifs that localizes to the inner membrane.
Article in FEBS letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Identification of proteins interacting with the N-terminal half of endoribonuclease RNase E inRNA biology · 2026Article
- Genetic adaptation to amoxicillin in Escherichia coli: The limited role of dinB and katE.PloS one · 2025Article
- Reverse-Phase Protein Microarrays for OverexpressedAnalytical chemistry · 2024Article
- Dynamic Protein Phosphorylation inMicroorganisms · 2024Article
- Defining Membrane Protein Topology Using pho-lac Reporter Fusions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Evaluation of small molecule kinase inhibitors as novel antimicrobial and antibiofilm agents.Chemical biology & drug design · 2021Review
- Extensive regulation of enzyme activity by phosphorylation in Escherichia coli.Nature communications · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In bacteria, signaling phosphorylation is thought to occur primarily on His and Asp residues. However, phosphoproteomic surveys in phylogenetically diverse bacteria over the past decade have identified numerous proteins that are phosphorylated on Ser and/or Thr residues. Consistently, genes encoding Ser/Thr kinases are present in many bacterial genomes such as in the Escherichia coli genome, which encodes at least three Ser/Thr kinases. Here, we identify a previously uncharacterized ORF, yegI, and demonstrate that it encodes a novel Ser/Thr kinase. YegI lacks several conserved motifs including residues important for Mg
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