Upon host (human neutrophil) infection interferes with productive FCAR signaling, inhibiting secreted IgA (SIgA) effector functions and probably avoiding neutrophil activation. Inhibits the SIgA-mediated oxidative burst by neutrophils, decreases generation of ROS (reactive oxygen species) by neutrophils and reduces chemotaxis by neutrophils, all of which are SIgA effector functions used to stimulate the immune response. Does not block SIgA-binding to its receptor (FCAR) on neutrophils, but it decreases SIgA-stimulated phosphorylation of cytoplasmic proteins, including phospholipase C-gamma and MAP kinases, all actions that may be advantageous to the pathogen. The physiological metal is unknown. Interacts with human secreted IgA (SIgA) at least via resides 244-260. Accumulates at 1 cell pole in the bladder of mice infected with this strain, in overexpressing bacteria the protein is found all over the cell surface but not in the secreted fraction (PubMed:23882011). Human blood sera from clinical patients with urinary tract infections reacts with antibodies to this protein (PubMed:23882011). More highly transcribed in logarithmic than stationary phase. Protein is not detected in bacteria growing in culture but is detected upon infection of mice (at protein level). Immunizes 1/3 of injected mice against subsequent infection with E.coli strain CFT073, suggesting it might be a good vaccine candidate for ExPEC (extraintestinal pathogenic E.coli) strains. Preferentially encoded in ExPEC strains (extraintestinal pathogenic E.coli).