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CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. CDI is neutralized by its cognate immunity protein CdiI, but not by non-cognate CdiI from other bacteria"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"The CdiA protein is thought to be exported from the cell through the central lumen of CdiB, the other half of its two-partner system (TPS). The TPS domain probably remains associated with CdiB while the FHA-1 domain forms an extended filament with the receptor-binding domain (RBD) at its extremity; in the secretion arrested state the C-terminus of the RBD and YP domains form a hairpin-like structure as the FHA-2, PT and CT domains are periplasmic. The YP domain is probably responsible for this arrest at the point where it re-enters the host cell periplasm. Upon binding to a target cell outer membrane receptor a signal is transmitted to activate secretion. The filament elongates slightly, the rest of CdiA is secreted and the FHA-2 domain becomes stably associated with the target cell's outer membrane where it facilitates entry of the toxic CT domain into the target cell periplasm. From there the toxic CT domain is cleaved and gains access to the target cell cytoplasm via an inner membrane protein"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21085179"}],"value":"Probably interacts with cognate immunity protein CdiI"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Secreted to the cell surface by CdiB, its two partner secretion pathway (TPS) partner (Probable)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Single-pass membrane protein","id":"SL-9904"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Target cell, target cell cytoplasm","id":"SL-0486"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21085179"}],"value":"The CDI activity resides in the approximately 220 residue C-terminal (CT) domain; exchanging the C-terminal (CT) domain and cdiI gene between different strains confers resistance within cognate but not non-cognate systems (i.e. CdiI-CO92 neutralizes CdiA-CT from strain CO92 but not CdiA-CT from E.coli strains 536 / UPEC, EC93 or from D.dadantii strain 3937)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the N-terminal section; belongs to the CdiA toxin family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":3295,"modifier":"EXACT"}},"description":"Toxin 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