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Background  Reversible protein phosphorylation catalyzed by protein kinases and phosphatases is the primary mechanism for signal transduction in all living organisms.  Streptococcus pneumoniae  encodes a single Ser/Thr protein kinase, StkP, which plays a role in virulence, stress resistance and the regulation of cell wall synthesis and cell division. However, the role of its cognate phosphatase, PhpP, is not well defined.    Results  Here, we report the successful construction of a Δ phpP  mutant in the unencapsulated  S. pneumoniae  Rx1 strain and the characterization of its phenotype. We demonstrate that PhpP negatively controls the level of protein phosphorylation in  S. pneumoniae  both by direct dephosphorylation of target proteins and by dephosphorylation of its cognate kinase, StkP. Catalytic inactivation or absence of PhpP resulted in the hyperphosphorylation of StkP substrates and specific phenotypic changes, including sensitivity to environmental stresses and competence deficiency. The morphology of the Δ phpP  cells resembled the StkP overexpression phenotype and conversely ,  overexpression of PhpP resulted in cell elongation mimicking the  stkP  null phenotype. Proteomic analysis of the  phpP  knock-out strain permitted identification of a novel StkP/PhpP substrate, Spr1851, a putative RNA-binding protein homologous to Jag. Here, we show that pneumococcal Jag is phosphorylated on Thr89. Inactivation of  jag  confers a phenotype similar to the  phpP  mutant strain.    Conclusions  Our results suggest that PhpP and StkP cooperatively regulate cell division of  S. pneumoniae  and phosphorylate putative RNA binding protein Jag.    Electronic supplementary material  The online version of this article (doi:10.1186/s12866-016-0865-6) contains supplementary material, which is available to authorized users.

bmc microbiology

Characterization of pneumococcal Ser/Thr protein phosphatase phpP mutant and identification of a novel PhpP substrate, putative RNA binding protein Jag