Tyrosine phosphorylation is a key device in numerous cellular functions in eukaryotes, but in
bacteria this protein modification was largely ignored until the mid-1990s. The first …

Phosphorylation events modify bacterial and archaeal proteomes, imparting cells with rapid
and reversible responses to specific environmental stimuli or niches. Phosphorylated …

Protein phosphorylation on tyrosine has been demonstrated to occur in a wide array of
bacterial species and appears to be ubiquitous among prokaryotes. This covalent …

Reversible protein phosphorylation is a major mechanism in the regulation of fundamental
signalling events in all living organisms. Bacteria have been shown to possess a versatile …

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 …

The ptp gene of Acinetobacter johnsonii was previously reported to encode a low-molecular-
mass protein, Ptp, whose amino acid sequence, predicted from the theoretical analysis of …

In this review, we address some recent developments in the field of bacterial protein
phosphorylation, focusing specifically on serine/threonine and tyrosine kinases. We present …

Acinetobacter johnsonii harbors a protein tyrosine kinase activity that is able to catalyze
autophosphorylation, like a number of eukaryotic tyrosine kinases. A biochemical and …

Reversible phosphorylation of serine, threonine and tyrosine residues by the interplay of
protein kinases and phosphatases plays a key role in regulating many different cellular …

Tyrosine phosphorylation is a common protein post-translational modification that plays a
critical role in signal transduction and the regulation of many cellular processes. Using a …