While recognized as an essential form of post-translational modification in eukaroytes, only in recent times has tyrosine phosphorylation been recognized as a key regulator of bacterial physiology and virulence. We have long studied a regulatory system comprising a protein tyrosine phosphatase (CpsB) and a protein tyrosine kinase (CpsD), focusing on its role in the regulation of capsule biosynthesis in Streptococcus pneumoniae. We were interested, however, in other roles this system may play in the physiology of this major human pathogen. Here, we show that the system plays a role in the LytA-dependent autolysis of the pathogen, with a mutant in CpsD undergoing autolysis at a significantly enhanced rate. This was not due to a difference in level of capsule, nor a result of increased sensitivity to endogenously added LytA. Furthermore, CpsD expression significantly increased during late stationary phase prior to the onset of autolysis, suggesting a role for the kinase at this stage of growth. We also show that LytA is tyrosine phosphorylated on Y264, and a substrate for both kinase CpsD, and phosphatase CpsB in vitro. Interestingly, we illustrate that this phosphorylation within the choline binding domain affects the ability of LytA to bind to choline analogues as well as to whole cell S. pneumoniae. Furthermore, we show that mutation of Y264 affects the ability of LytA to form higher order oligomers, likely due to differences in the ability to bind choline. Finally, phospho-ablative mutation on the chromosome (Y264F) prolongs time before autolysis of the culture, while phosphomimetic mutation (Y264E) enhanced autolysis. This work provides an interesting new link between the regulation of capsule biosynthesis, and the characteristic autolysis of the pneumococcus, while illustrating the fundamental importance of tyrosine phosphorylation to the physiology of this major human pathogen.