The carbohydrate-uptake phosphorelay PTS system plays a key role in metabolic regulation in Bacteria controlling the utilization of secondary carbon sources. Some Bacteria, such as Escherichia coli, encode a paralogue system named PTSNtr (nitrogen related PTS). PTSNtr is composed of EINtr (ptsP), NPr (ptsO), and EIIANtr (ptsN). These proteins act as a phosphorely system transfering phosphoryl from phosphoenolpyruvate to EINtr, NPr and them to EIIANtr. PTSNtr is not involved in carbohydrate uptake and it may be dedicated to play regulatory functions. The phosphorylation state of the EINtr is regulated by allosteric binding of glutamine and 2-oxoglutarate, metabolites whose intracellular levels reflect the nitrogen levels. Despite the denomination and nitrogen-sensory properties no major effect of PTSNtr on nitrogen regulation has been described in E. coli. Here we show that an E. coli ∆ptsN has impaired growth in minimal medium. Proteome analysis of the ∆ptsN strain under different nitrogen regimes revealed that ptsN is not involved in the regulation of the canonical nitrogen starvation response. The proteomic data support that ptsN is required for proper balance between RpoS and sigma 70 activities such that, in the absence of ptsN, RpoS-depended genes are preferentially expressed.