Responsible for autoagglutination, and for adhesion to abiotic and biotic surfaces such as polystyrene (PS), type I collagen, polypropylene (PP), polyvinylchloride (PVC), glass and stainless steel (SS). Adhesion is much stronger than that mediated by Yersinia YadA in a comparative assay. Confers autoagglutination and binding to PS, type I collagen, PP, PVC, glass and SS upon expression in Acinetobacter baylyi strain ADP1 (PubMed:23155410). Involved in rapid, irreversible adherence to polyurethane (PubMed:17090933). Forms an unusual biofilm (PubMed:31972092). An extended, surface exposed fiber binds to quartz crystals, PS and glass. It can be removed by washing in distilled water (PubMed:27305955, PubMed:28720107). Homotrimer (PubMed:26698633) (Probable). Interacts with TpgA (PubMed:27074146). Localizes to thin, peritrichate nanofibers (200 nm long, 3.5 nm diameter) on the cell surface; an antibody against residues 699-1014 only labels the distal tip of these fibers (PubMed:23155410, PubMed:27074146). The C-terminal translocator domain is probably localized in the outer membrane (Probable). Part of the ataA-tpgA operon. The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, trimerization and 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 (By similarity). Seems to have 2 tandemly fused passenger domains; a long N-terminal one (residues 59-2904) and a shorter C-terminal one (residues 2905-3561) (Probable). The C-terminal passenger domain is an entwined, elongated trimer about 450 Angstroms in length that is rigid and yet able to bend somewhat. The ability to bind biotic and abiotic substrates lies in the N-terminal passenger domain (PubMed:26698633). The isolated, trimeric, passenger domain (residues 24-3487) forms fibers 225 nm in length, 4 nm in diameter and has a globular structure at both its N-terminus and near its C-terminus. Its secondary structure is resistant to heat up to 80 degrees Celsius, to treatment at pH 2 and 12, as well as incubation in 0.1 M HCl. The intact fibers adhere rapidly to a quartz crystal microbalance system; heat denatured fibers bind less well as their secondary structure decreases (PubMed:27305955). Targeted small domain deletions show the fine ultrastructure of the fiber (PubMed:27305955). Loss of rapid, irreversible adhesion to polyurethane, loss of both an anchor-like appendage and a peritrichate fibril-type appendage on the cell surface (PubMed:17090933, PubMed:23155410). Cells retain type 1 and Fil fimbriae (defined by FimA and FilA protein respectively) (PubMed:23155410). Can be used to immobilize bacteria on a solid support; cells can be removed by washing in distilled water, and will reattach as the ionic strength of the medium increases above 10 mM. The attach-detach cycle can be repeated at least 4 times, each time the cells reattach as well as the first time (PubMed:23893702, PubMed:28720107). Expression in the indigo-producing Acinetobacter strain ST-550 leads to cell adherence to a support material and subsequently 5-fold increased levels of indigo production (PubMed:23893702). Insertion of a human rhinovirus protease 3C site allows isolation of the intact, folded passenger domain after protease treatment of whole cells. The protease cuts in the tag as indicated GGGLEVLFLQ|GPG. Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.