%0 Journal Article %A Ahmad, Zuleeza %A Morona, Renato %A Standish, Alistair J. %T In vitro characterization and identification of potential substrates of a low molecular weight protein tyrosine phosphatase in Streptococcus pneumoniae %D 2018 %J Microbiology, %V 164 %N 4 %P 697-703 %@ 1465-2080 %R https://doi.org/10.1099/mic.0.000631 %K low molecular weight phosphatase %K Streptococcus pneumoniae %K tyrosine phosphorylation %K pneumococcus %K phosphatase substrates identification %I Microbiology Society, %X Streptococcus pneumoniae is a major human pathogen responsible for significant mortality and morbidity worldwide. Within the annotated genome of the pneumococcus lies a previously uncharacterized protein tyrosine phosphatase which shows homology to low molecular weight protein tyrosine phosphatases (LMWPTPs). LMWPTPs modulate many processes critical for the pathogenicity of a number of bacteria including capsular polysaccharide biosynthesis, stress response and persistence in host macrophages. Here, we demonstrate that Spd1837 is indeed a LMWPTP, by purifying the protein, and characterizing its phosphatase activity. Spd1837 showed specific tyrosine phosphatase activity, and it did not form higher order oligomers in contrast to many other LMWPTPs. Substrate-trapping assays using the wild-type and the phosphatase-deficient Spd1837 identified potential substrates/interacting proteins including major metabolic enzymes such as ATP-dependent-6-phosphofructokinase and Hpr kinase/phosphorylase. Given the tight association between the bacterial basic physiology and virulence, this study hopes to prompt further investigation of how the pneumococcus controls its metabolic flux via the LMWPTP Spd1837. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.000631