The universal stress protein, UspA, of Escherichia coli is phosphorylated in response to stasis.

Transcriptional induction of the uspA gene of Escherichia coli occurs whenever conditions cause growth arrest and cells deficient in UspA survive poorly in stationary phase. We demonstrate that the product of uspA is a serine and threonine phosphoprotein. In vivo, three isoforms of UspA were detected, two of which were phosphorylated as determined by alkaline phosphatase treatment; in vitro, phosphorylation with [gamma-32P]ATP yielded two radioactive UspA isoforms. The phosphorylated isoforms were barely visible in growing cells but one increased during starvation conditions causing growth arrest. This phosphorylation is dependent on the o591 gene, which encodes an autophosphorylating tyrosine phosphoprotein and which is involved in the synthesis or modification of six other proteins. In vitro, UspA undergoes a rapid and dynamic autophosphorylation, as shown by chase experiments with GTP or ATP as phosphate donors.