Many virulence factors of Gram-positive bacteria are anchored to the peptidoglycan by a sorting signal. While surface display mechanisms are well characterized, less is known about the spatial and temporal organization of these proteins in the bacterial envelope. This review summarizes recent studies on the rod-shaped Listeria monocytogenes, ovococcal Streptococcus pyogenes and spherical Staphylococcus aureus bacteria that provide insights into the compartmentalization of the surface and distribution of peptidoglycan-anchored proteins in space and time. We discuss models that support mechanistic bases for localization of proteins at the poles, septum or lateral sites. The results indicate that deployment of virulence factors by pathogenic bacteria is a dynamic process tightly connected to secretion, cell morphogenesis, cell division rate and gene expression levels.