Premium
Escherichia coli YegI is a novel Ser/Thr kinase lacking conserved motifs that localizes to the inner membrane
Author(s) -
Rajagopalan Krithika,
Dworkin Jonathan
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13920
Subject(s) - escherichia coli , kinase , biology , phosphorylation , conserved sequence , bacterial genome size , genome , protein serine threonine kinases , gene , biochemistry , membrane protein , bacteria , microbiology and biotechnology , genetics , peptide sequence , protein kinase a , membrane
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 2+ binding seen in other bacterial Ser/Thr kinases, suggesting that the consensus may be too stringent. We further find that YegI is a two‐pass membrane protein with both N‐ and C termini located intracellularly.