Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes attachment to eukaryotic cells and after invasion, is the major adhesin in infected tissue. Constitutes an alternative uptake pathway under conditions in which invasin synthesis is repressed. Homotrimer. The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface. Induced at 37 degrees Celsius by the temperature-dependent transcriptional activator LcrF (VirF). 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. Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.