Non-specific FomA porin precursor (Kleivdal et al. 1995). The N-terminal region is periplasmic while the C-terminus is a 14 stranded β-barrel (Puntervoll et al. 2002).  The β-barrel may have a tilt angle of 45° relative to the barrel axis (Anbazhagan et al., 2008). FomA is fusogenic (Pszon-Bartosz et al., 2011).  Its unique solute transport activity with size exclusion limit has been described (Kattner et al. 2015). FomA is a voltage-dependent porin, predicted to form a 14 stranded beta-barrel. It folds in a range of model membranes of very different phospholipid compositions. A study on FomA folding into lipid bilayers indicated the presence of parallel folding pathways for OMPs with larger transmembrane beta-barrels (Kleinschmidt 2006).