Surface proteins are essential components of bacteria-environment interactions. Akin to their cytoplasmic counterparts, polar localization of surface proteins is required in many contexts such as cell infection or biofilm formation. However, live imaging studies of Outer Membrane Proteins (OMP) in the Gram-negative bacterium E. coli have revealed that OMP are inserted homogeneously on the lateral surface. Despite passive advection to bacterial poles by addition of new cell wall material and reduced polar diffusion, only old proteins accumulate efficiently but slowly at bacterial poles. Here we show how the dynamics in the periplasmic space between the inner and the outer membrane actively localize Ag43, an E. coli OMP involved in cell-cell adhesion, to bacterial poles. The periplasmic dynamics was captured by a Fokker-Planck equation that account for inhomogeneous drift and diffusion. We further demonstrated that the dynamics of periplasmic Ag43 is coupled to the Min system, whose cytoplasmic components are known to oscillate from pole to pole during the cell cycle.  Our results suggest that different pathways co-exist for OMP positioning and that the Min system not only organize cytoplasmic components but also contributes to the organization of OMP on the cell envelope.