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Once entered into host cells, acidification in the endosome promotes the membrane insertion of the translocation region and formation of a pore, leading to translocation of the GT44 and peptidase C80 domains across the endosomal membrane (By similarity). This activates the peptidase C80 domain and autocatalytic processing, releasing the N-terminal part (N-acetylglucosaminyltransferase TcdA), which constitutes the active part of the toxin, in the cytosol (PubMed:17334356)"}],"commentType":"FUNCTION","molecule":"Toxin A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8810274"}],"value":"Active form of the toxin, which is released into the host cytosol following autoprocessing and inactivates small GTPases (PubMed:16157585, PubMed:8810274). Acts by mediating monoglycosylation of small GTPases of the Rho family (Rac1, RhoA, RhoG and Cdc42) in host cells at the conserved threonine residue located in the switch I region ('Thr-37/35'), using UDP-N-acetyl-alpha-D-glucosamine as the sugar donor (PubMed:16157585, PubMed:8810274). 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Acidification in the endosome triggers conformational changes that promote the membrane insertion of the translocation region, allowing formation of a pore, leading to translocation of the GT44 and peptidase C80 domains across the endosomal membrane (By similarity). 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C80 domain and autoprocessing, generating the N-acetylglucosaminyltransferase TcdA form, which is released in the host cytosol (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20498856"}],"value":"Host endosome membrane","id":"SL-0394"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"N-acetylglucosaminyltransferase TcdA","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q46342"}],"value":"Binding to phospholipids, such as phosphatidylserine and phosphatidic acid promotes localization to the inner face of the cell membrane close to its membrane anchored substrates (small GTPases)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"value":"Host cytoplasm, host cytosol","id":"SL-0384"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q46342"}],"value":"Host cell membrane","id":"SL-0375"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q46342"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q46342"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29146177"}],"value":"Consists of 4 functional domains: (1) the N-terminal GT44 domain (glycosyltransferase, also named GTD), which mediates glucosylation of host small GTPases, (2) an autoprocessing region that catalyzes autoprocessing to release the N-terminal GT44 domain in the host cytosol, (3) the translocation region that forms a pore to promote translocation of the GT44 and peptidase C80 domains across the endosomal membrane and (4) the receptor-binding (CROPS) region that mediates binding to host cells and contribute to entry into cells"}],"commentType":"DOMAIN","molecule":"Toxin A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"value":"The receptor-binding (CROPS) region is dynamic and can have open and closed conformations depending of the pH: has an open conformation at endosomal pH and a closed conformation at neutral pH"}],"commentType":"DOMAIN","molecule":"Toxin A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P16154"}],"value":"The cell wall-binding repeats bind carbohydrates, probably contributing to entry into cells"}],"commentType":"DOMAIN","molecule":"Toxin A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q46342"}],"value":"The four-helical bundle region mediates binding to phospholipids, such as phosphatidylserine and phosphatidic acid (By similarity). 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