Hyperproduction of phosphate‐binding protein, PhoS, in strains carrying a multicopy plasmic containing the phoS gene, resulted in saturation of export sites. As a consequence, pre‐PhoS was accumulated both in the inner membrane and in the cytoplasm. This was evidenced both in electron‐microscopy and after cell fractionation. Only the membrane‐associated precursor could be matured and exported. The signal sequence of the cytoplasmic pre‐PhoS was slowly degraded. It was first cleaved about in its middle and then completely removed. Electron microscope studies demonstrated that the cytoplasmic pre‐PhoS cannot be exported post‐translationally.