Minireviews
Microbial Protein-tyrosine Kinases*

https://doi.org/10.1074/jbc.R113.520015Get rights and content
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Microbial ester kinases identified in the past 3 decades came as a surprise, as protein phosphorylation on Ser, Thr, and Tyr amino acids was thought to be unique to eukaryotes. Current analysis of available microbial genomes reveals that “eukaryote-like” protein kinases are prevalent in prokaryotes and can converge in the same signaling pathway with the classical microbial “two-component” systems. Most microbial tyrosine kinases lack the “eukaryotic” Hanks domain signature and are designated tyrosine kinases based upon their biochemical activity. These include the tyrosine kinases termed bacterial tyrosine kinases (BY-kinases), which are responsible for the majority of known bacterial tyrosine phosphorylation events. Although termed generally as bacterial tyrosine kinases, BY-kinases can be considered as one family belonging to the superfamily of prokaryotic protein-tyrosine kinases in bacteria. Other members of this superfamily include atypical “odd” tyrosine kinases with diverse mechanisms of protein phosphorylation and the “eukaryote-like” Hanks-type tyrosine kinases. Here, we discuss the distribution, phylogeny, and function of the various prokaryotic protein-tyrosine kinases, focusing on the recently discovered Mycobacterium tuberculosis PtkA and its relationship with other members of this diverse family of proteins.

Bacterial Protein Kinases
Bacterial Signal Transduction
Signal Transduction
Signaling
Protein-tyrosine Kinase (Tyrosine Kinase)
BY-kinases
Mycobacterium tuberculosis PtkA
Tyr Kinase

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*

This work was supported by Canadian Institutes of Health Research (CIHR) Operating Grant MOP-106622. This is the first article in the Thematic Minireview Series “Protein Serine/Threonine and Tyrosine Phosphorylation in Prokaryotes.”

This article contains supplemental Figs. S1 and S2.