In Gram-negative bacteria, beta-barrel proteins are integrated into the outer membrane by the beta-barrel assembly machinery, with key components of the machinery being the Omp85 family members BamA and TamA. Recent crystal structures and cryo-electron microscopy show a diverse set of secretion pores in Gram-negative bacteria, with alpha-helix (Wza, GspD) or beta-strand (CsgG) transmembrane segments in the outer membrane. We developed assays to measure the assembly of three distinct secretion pores that mediate protein (GspD), curli fibre (CsgG) and capsular polysaccharide (Wza) secretion by bacteria, and show that depletion of BamA and TamA does not diminish the assembly of Wza, GspD or CsgG. Like the well characterized pilotins for GspD and other secretins, small periplasmic proteins enhance the assembly of the CsgG beta-barrel. We discuss a model for integral protein assembly into the bacterial outer membrane, focusing on the commonalities and differences in the assembly of Wza, GspD and CsgG.