Binds (in a non-immune fashion) to the Fc portion of human IgG and less well to IgA; binding occurs on the cell surface. Confers the ability to survive exposure to human serum exposure (PubMed:10722621). Binds to the Fc portion of human IgG and IgA and to whole mouse antibodies also via Fc (PubMed:19303642). Homotrimer; can probably form mixed heterotrimers in vivo (PubMed:22155776). Will form mixed heterotrimers with EibD; these are correctly located in the outer membrane and bind IgG Fc, although less well than homotrimers (PubMed:22155776). In denaturing gels runs as a band of about 200 kDa (PubMed:10722621). Binds the Fc portion of immunoglobulins; binds more than 1 Fc per subunit (PubMed:19303642). 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 (By similarity). 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 (PubMed:22155776). Trimerizes to make a lollipop-shaped form which consists of three domains: a C-terminal membrane-anchor domain, an extended coiled-coil stalk domain which binds IgG Fc, and an N-terminal head domain (By similarity). Encoded in a prophage region of strain ECOR 9, upon UV treatment bacteriophage containing this gene can be isolated. Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family. Eib subfamily.