This work focus on  in the role of Ser/Thr/Tyr protein phosphorylation in Streptococcus thermophilus, the only streptococcal species used in food fermentation. During technological processes, S. thermophilus has to adapt to various nutrition and physical-chemical stresses that require rapid adjustments. In this study, we investigated a way for S. thermophilus to regulate specific pathways namely post-translational protein modifications and more specifically protein serine/threonine/tyrosine phosphorylation. We would like to assess the specific role of the only predicted Hanks-type kinase, named PknB. We performed in parallel a global shotgun proteomics and a specific phosphoproteomics analyses on both the wild type strain and its Hanks-type kinase deletion mutant. All the analysis were performed on an Orbitrap Fusion Lumos Tribrid. We showed that the S. thermophilus Ser/Thr/Tyr phosphoproteome is of the same order of magnitude than the other streptococci ones as peptides belonging to 106 proteins (410 phosphopeptides corresponding to 161 peptide sequences with different phosphosite positions) from various metabolic pathways were found phosphorylated in one bacterial growth condition. The phosphorylation occurred for 43 % on serine, 33 % on threonine and 23 % on tyrosine.  We demonstrated that the Hanks-type kinase, named PknB in S. thermophilus, targets the divisome and is only one of the players in the Ser/Thr/Tyr phosphorylation process. Consistent with these results, the pknB deletion mutant exhibits a clear phenotype with longer whimsical chains and affected division process.