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Static versus dynamic adherence results differ slightly; in dynamic adherence studies bacteria bind to fixed components under a constant defined flow rate to simulate in vivo infection conditions (PubMed:15534369, PubMed:17060468, PubMed:18627378, PubMed:21536788, PubMed:23163798). Induces secretion of host pro-angiogenic cytokines such as VEGFA, ADM, IGFBP-3 and IL-8. May prevent bacterial phagocytosis by macrophages (Probable) (PubMed:15534369). Probably mediates bacterial autoagglutination (PubMed:17060468, PubMed:18627378). Negatively impacts type IV secretion system effectors (VirB/D4 T4SS and its substrate Bep proteins), possibly by preventing close association of host and bacterial cells. This implies the 2 factors are expressed at different times during infection (Probable)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18688279"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"18688279"}],"value":"Homotrimer (Probable). Crystals of the head region form trimers (PubMed:18688279)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C2W0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15534369"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18627378"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21536788"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21981119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23163798"}],"value":"Forms long (about 240 nm) filaments extending from the cell surface, which were initially called type IV pili (PubMed:15534369, PubMed:18627378, PubMed:21536788, PubMed:21981119, PubMed:23163798). The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15534369"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18627378"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21536788"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21981119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23163798"}],"value":"Cell surface","id":"SL-0310"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15534369"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18627378"}],"value":"Cell outer membrane","id":"SL-0040"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18627378"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21981119"}],"value":"The N-terminus (residues 48-376) performs most of the host-associated functions of the protein and binds collagen. The large central domain (composed of neck-stalk repeats about residue 470-2850) is required to bind host fibronectin and contributes to host cell adherence, collagen-binding and induction of host pro-angiogenic factors"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C2W0"}],"value":"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"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15534369"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21536788"}],"value":"No longer binds to host cells or host extracellular matrix proteins, loss of bacterial 'type IV-like pili'. Bacteria are more frequently phagocytosed by murine J774 macrophages. Infected HeLa cells no longer secrete pro-angiogenic factors such as VEGFA, ADM, IGFBP3 or IL-8 (PubMed:15534369). Decreased binding to host epithelial cells and to host extracellular matrix components vitronectin, hyaluronate, fibronectin, laminin, collagens I, III and IV under static and dynamic flow conditions (PubMed:21536788)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15534369"}],"value":"Antisera to this protein are frequently present in humans and animals infected by B.henselae, suggesting it might be useful as a marker for B.henselae infection"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Infection with B.henselae leads to cat scratch disease in immunocompetent individuals and bacillary angiomatosis, tumorous proliferations of endothelial cells in the skin and internal organs in immunocompromised patients"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) 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