Involved in adhesion of capsulated meningococci to host epithelial cells. Interacts with laminin and heparan sulfate, promoting the adherence to the extracellular matrix (ECM) components. Homotrimer. The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface. The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface. Deletion of the gene decreases the ability to adhere to Chang epithelial cells. Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.