When considering protein phosphorylation in bacteria, phosphorylation of aspartic acid and histidine residues mediated by the two-component systems is the first to spring to mind. And yet other phosphorylation systems have been described in bacteria in the past 20 years including eukaryotic-like serine/threonine kinases and more recently tyrosine-kinases. Among the latter, a peculiar type is widespread among bacteria, but not in higher organisms. These enzymes possess unique structural features defining thus a new family of enzymes termed Bacterial tyrosine kinases (BY-kinases). BY-kinases have been shown to be mainly involved in polysaccharide production, but their ability to phosphorylate endogenous substrates indicates that they participate in the regulation of other functions of the bacterial cell. Recent advances in mass spectrometry based phosphoproteomics provided lists of many new phosphotyrosine-proteins, indicating that BY-kinases may be involved in regulating a large array of other cellular functions. One may expect that in a near future, tyrosine phosphorylation will turn out to be one of the key regulatory processes in the bacterial cell and will yield new insights into the understanding of its physiology.