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 …

Two proteins of Klebsiella pneumoniae, termed Yor5 and Yco6, were analyzed for their
capacity to participate in the reversible phosphorylation of proteins on tyrosine. First, protein …

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 …

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 …

The predicted protein product of open reading frame slr0328 from Synechocystis sp. PCC
6803, SynPTP, possesses significant amino acid sequence similarity with known low …

A putative low molecular weight protein tyrosine phosphatase (LMW‐PTP) was identified in
the genome sequence of the bacterial pathogen, Campylobacter jejuni. This novel gene …

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

The analysis of the different amino acid sequences deduced from the complete genome
sequence of the gram-positive bacterium Staphylococcus aureus suggested the presence of …

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

We have isolated a cDNA of a novel cytoplasmic variant of the protein tyrosine phosphatase
ϵ (PTPϵ) from rat spleen cDNA library. Its deduced amino acid sequence of 642 residues …