Bacterial cell division is a complex and highly regulated process requiring the coordination of many different proteins. Despite substantial work in model organisms, our understanding of the systems regulating cell division in non-canonical organisms, including critical human pathogens, is far from complete. One such organism is Staphylococcus aureus, a spherical bacterium that lacks known cell division regulatory proteins. Recent studies on GpsB, a protein conserved within the Firmicutes phylum, have provided insight into cell division regulation in S. aureus and other related organisms. It has been revealed that GpsB coordinates cell division and cell wall synthesis in multiple species by interacting with Penicillin Binding Proteins (PBPs) and other partners. In S. aureus, we have previously shown that GpsB directly regulates FtsZ polymerization. In this study, using Bacillus subtilis as a tool, we isolated intragenic and extragenic spontaneous suppressor mutants that abrogate the lethality of S. aureus GpsB overproduction in B. subtilis. Through characterization of these mutants, we identified several key residues important for the function of GpsB. Furthermore, we discovered an additional role for GpsB in wall teichoic acid (WTA) biosynthesis in S. aureus. Specifically, we show that GpsB directly interacts with the wall teichoic acid export protein TarG using a bacterial two-hybrid analysis. We also identified a three-residue motif in GpsB that is crucial for this interaction. Based on the analysis of the localization of TagG in B. subtilis and its homolog TarG in S. aureus, it appears that WTA machinery is a part of the divisome complex. As such, we show additional evidence to the growing body of work that suggests that along with peptidoglycan synthesis, WTA biosynthesis and export may take place at the site of cell division. Taken together, this research illustrates how GpsB performs an essential function in S. aureus by directly linking the tightly regulated cell cycle processes of cell division and WTA-mediated cell surface decoration.