Participates in bacterial attachment to several surfaces, including various extracellular matrix (ECM) components and a hydrophobic abiotic surface. Involved in adhesion to host epithelial cells and is required for full virulence in mice. Also implicated in the resistance to porcine serum. Homotrimer. The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface (By similarity). Localizes at the new cell pole generated after cell division (PubMed:24236157). 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 mutant shows a significant decrease in the attachment to an abiotic surface and in the ability to bind collagen, hyaluronic acid and fetuin. Deletion leads to decreased adhesion to host cells, but it does not affect later stages of cellular infection. Splenic infection is significantly reduced in mice. Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.