the cytoplasmic and membrane bound parts of the peptidoglycan biosynthetic pathway converge to the forespore membrane and may also form a cardiolipin-dependent metabolic supercomplex. Such complex could serve to channel metabolic precursors and enhance the efficiency of the peptidoglycan synthesis pathway. It is becoming increasingly clear that protein supercomplexes, such as the divisome, are important in a large number of bacterial biological processes (Rudner et al., 2002). Mislocalization of these proteins directly affects enzyme activity. Enzymes unable to localize properly may not be able to reach their target substrate. They may also be unable to bind activating protein partners. In cases where substrate is still present, the enzyme may not be generating product in a location useful to the cell. We provide further evidence through MurG that enzyme localization in bacteria is critical to its function