{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P16154","secondaryAccessions":["M4NKU2"],"uniProtkbId":"TCDA_CLODI","entryAudit":{"firstPublicDate":"1990-04-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-02-01","entryVersion":135,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Clostridioides difficile","commonName":"Peptoclostridium difficile","taxonId":1496,"lineage":["Bacteria","Bacillati","Bacillota","Clostridia","Peptostreptococcales","Peptostreptococcaceae","Clostridioides"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2109310"}],"value":"Toxin A"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334356"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19553670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27571750"}],"value":"3.4.22.-"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Glucosyltransferase TcdA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22267739"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24905543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30622517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7775453"}],"value":"2.4.1.-"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"24958798"}],"value":"tcdA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2109310"}],"value":"toxA"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16622409"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1670930"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334356"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19252482"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19553670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20844489"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27571750"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27680706"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31160825"}],"value":"Precursor of a cytotoxin that targets and disrupts the colonic epithelium, inducing the host inflammatory and innate immune responses and resulting in diarrhea and pseudomembranous colitis (PubMed:20844489). TcdA and TcdB constitute the main toxins that mediate the pathology of C.difficile infection, an opportunistic pathogen that colonizes the colon when the normal gut microbiome is disrupted (PubMed:19252482, PubMed:20844489). Compared to TcdB, TcdA is less virulent and less important for inducing the host inflammatory and innate immune responses (PubMed:19252482). This form constitutes the precursor of the toxin: it enters into host cells and mediates autoprocessing to release the active toxin (Glucosyltransferase TcdA) into the host cytosol (By similarity). Targets colonic epithelia by binding to some receptor, and enters host cells via clathrin-mediated endocytosis (By similarity). Binding to LDLR, as well as carbohydrates and sulfated glycosaminoglycans on host cell surface contribute to entry into cells (PubMed:16622409, PubMed:1670930, PubMed:31160825). In contrast to TcdB, Frizzled receptors FZD1, FZD2 and FZD7 do not act as host receptors in the colonic epithelium for TcdA (PubMed:27680706). 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 (Glucosyltransferase TcdA), which constitutes the active part of the toxin, in the cytosol (PubMed:17334356, PubMed:19553670, PubMed:27571750)"}],"commentType":"FUNCTION","molecule":"Toxin A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22267739"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24905543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30622517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7775453"}],"value":"Active form of the toxin, which is released into the host cytosol following autoprocessing and inactivates small GTPases (PubMed:22267739, PubMed:22747490, PubMed:24905543, PubMed:30622517, PubMed:7775453). Acts by mediating monoglucosylation of small GTPases of the Rho family (Rac1, RhoA, RhoB, RhoC, Rap2A and Cdc42) in host cells at the conserved threonine residue located in the switch I region ('Thr-37/35'), using UDP-alpha-D-glucose as the sugar donor (PubMed:22267739, PubMed:22747490, PubMed:24905543, PubMed:30622517, PubMed:7775453). Monoglucosylation of host small GTPases completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption and cell death, resulting in the loss of colonic epithelial barrier function (PubMed:7775453). Also able to catalyze monoglucosylation of some members of the Ras family (H-Ras/HRAS, K-Ras/KRAS and N-Ras/NRAS), but with much less efficiency than with Rho proteins, suggesting that it does not act on Ras proteins in vivo (PubMed:30622517)"}],"commentType":"FUNCTION","molecule":"Glucosyltransferase TcdA"},{"commentType":"CATALYTIC ACTIVITY","molecule":"Glucosyltransferase TcdA","reaction":{"name":"L-threonyl-[protein] + UDP-alpha-D-glucose = 3-O-(alpha-D-glucosyl)-L-threonyl-[protein] + UDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:64684"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:16656"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:58223"},{"database":"ChEBI","id":"CHEBI:58885"},{"database":"ChEBI","id":"CHEBI:156085"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22267739"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24905543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30622517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7775453"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:64685"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22267739"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24905543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30622517"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7775453"}]}]},{"commentType":"COFACTOR","molecule":"Toxin A","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27571750"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27571750"}],"value":"Binds 1 Zn(2+) ion per subunit (PubMed:27571750). Zn(2+) is required for autocatalytic cleavage (PubMed:27571750)."}]}},{"commentType":"COFACTOR","molecule":"Glucosyltransferase TcdA","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22267739"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28433497"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"}],"value":"Has higher activity with Mn(2+), but most likely uses Mg(2+) in host cells (By similarity). Required for glucosyltransferase activity (PubMed:22747490)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334356"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19553670"}],"value":"Protease activity is activated upon binding to 1D-myo-inositol hexakisphosphate (InsP6), which induces conformational reorganization"}],"commentType":"ACTIVITY REGULATION","molecule":"Toxin A"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","molecule":"Glucosyltransferase TcdA","kineticParameters":{"maximumVelocities":[{"velocity":252.2,"unit":"pmol/min/ug","enzyme":"enzyme with UDP-alpha-D-glucose (in presence of K(+))","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"}]},{"velocity":162.8,"unit":"pmol/min/ug","enzyme":"enzyme with UDP-alpha-D-glucose (in presence of NH4(+))","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"}]},{"velocity":36.4,"unit":"pmol/min/ug","enzyme":"enzyme with UDP-alpha-D-glucose (in presence of Na(+))","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"}]}],"michaelisConstants":[{"constant":43.9,"unit":"uM","substrate":"UDP-alpha-D-glucose (in presence of K(+))","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"}]},{"constant":36.3,"unit":"uM","substrate":"UDP-alpha-D-glucose (in presence of NH4(+))","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"}]},{"constant":51.1,"unit":"uM","substrate":"UDP-alpha-D-glucose (in presence of Na(+))","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22747490"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31160825"}],"value":"Interacts with host LDLR; LDLR probably does not constitute a major receptor but may contribute to entry into cells"}],"commentType":"SUBUNIT","molecule":"Toxin A"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Toxin A","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19553670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20498856"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22685398"}],"value":"Secreted from C.difficile cell into the extracellular environment via help of holin-like protein TcdE/UtxA (PubMed:22685398). Binds to the cell surface receptors via the receptor-binding region and enters the cells via clathrin-mediated endocytosis (PubMed:20498856). 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 Glucosyltransferase TcdA form, which is released in the host cytosol (PubMed:19553670)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22685398"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"value":"Host endosome membrane","id":"SL-0394"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Glucosyltransferase 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 (glucosyltransferase, 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:0000269","source":"PubMed","id":"16622409"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"1670930"}],"value":"The cell wall-binding repeats bind carbohydrates, such as Galalpha1-3Galbeta1-4GlcNAc, probably contributing to entry into cells"}],"commentType":"DOMAIN","molecule":"Toxin A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q46342"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25882477"}],"value":"The four-helical bundle region mediates binding to phospholipids, such as phosphatidylserine and phosphatidic acid (PubMed:25882477). This promotes localization to the inner face of the cell membrane close to small GTPases (By similarity)"}],"commentType":"DOMAIN","molecule":"Glucosyltransferase TcdA"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334356"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19553670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22267739"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27571750"}],"value":"Undergoes autocatalytic cleavage to release the N-terminal part (Glucosyltransferase TcdA), which constitutes the active part of the toxin, in the host cytosol (PubMed:17334356, PubMed:19553670, PubMed:22267739, PubMed:27571750). 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C80 domain and promotes autoprocessing (PubMed:17334356, PubMed:19553670)"}],"commentType":"PTM","molecule":"Toxin A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20844489"}],"value":"Cells lacking tcdA display virulence and cytotoxicity, because of the presence of TcdB (PubMed:20844489). Cells lacking both tcdA and tcdB display a strongly reduced virulence (PubMed:20844489)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the clostridial glucosylating toxin (LCGT) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18411291"},{"evidenceCode":"ECO:0000305"}],"value":"Host HSP90B1/gp96 was initially identified as a possible receptor for TcdA (PubMed:18411291). However, as HSP90B1/gp96 localizes in the endoplasmic reticulum and not at the cell membrane, it probably does not act as a receptor for TcdA"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":2710,"modifier":"EXACT"}},"description":"Toxin A","featureId":"PRO_0000072634"},{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":542,"modifier":"EXACT"}},"description":"Glucosyltransferase TcdA","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19553670"}],"featureId":"PRO_0000451191"},{"type":"Domain","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"GT44","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Domain","location":{"start":{"value":569,"modifier":"EXACT"},"end":{"value":776,"modifier":"EXACT"}},"description":"Peptidase 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Active toward 4-hydroxyphenylacetate, 3,4-dihydroxyphenylacetate and to a lesser extent p-hydroxymandelate (2-hydroxy-2-(4-hydroxyphenyl)acetate), forming 4-methylphenol, 4-methylcatechol and 4-hydroxybenzylalcohol, respectively. Is likely involved in the catabolism of aromatic amino acids such as tyrosine fermentation. 4-methylphenol (p-cresol) formation provides metabolic toxicity, which may benefit the pathogen C.difficile by suppression of the endogenous gastrointestinal microflora, allowing the development of gastrointestinal infections (PubMed:11231288, PubMed:16878993). The large subunit is the catalytic subunit that binds the substrate (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-hydroxyphenylacetate + H(+) = 4-methylphenol + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22732"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:17847"},{"database":"ChEBI","id":"CHEBI:48999"}],"ecNumber":"4.1.1.83","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11231288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:22733"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11231288"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"16878993"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3,4-dihydroxyphenylacetate + H(+) = 4-methylcatechol + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:62556"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:17254"},{"database":"ChEBI","id":"CHEBI:17612"}],"ecNumber":"4.1.1.83","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11231288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:62557"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11231288"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"16878993"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-hydroxy-2-(4-hydroxyphenyl)acetate + H(+) = 4-hydroxybenzyl alcohol + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:62588"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:32804"},{"database":"ChEBI","id":"CHEBI:67410"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11231288"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:62589"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11231288"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11231288"}],"value":"Enzyme activity catalyzed by the HPA decarboxylase complex is rapidly and irreversibly inactivated by oxygen. Competitively inhibited by p-hydroxyphenylacetamide. Not inhibited by m- or o-hydroxyphenyl-acetate, p-hydroxybenzoate or p-hydroxyphenylpropionate"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":14.97,"unit":"umol/min/mg","enzyme":"enzyme for the decarboxylation of 4-hydroxyphenylacetate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}]},{"velocity":8.82,"unit":"umol/min/mg","enzyme":"enzyme for the decarboxylation of 3,4-hydroxyphenylacetate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}]}],"michaelisConstants":[{"constant":649.0,"unit":"uM","substrate":"4-hydroxyphenylacetate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}]},{"constant":410.0,"unit":"uM","substrate":"3,4-dihydroxyphenylacetate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}],"value":"kcat is 110 sec(-1) for the decarboxylation of 4-hydroxyphenylacetate. kcat is 65 sec(-1) for the decarboxylation of 3,4-hydroxyphenylacetate."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11231288"}],"value":"Optimum pH is 7.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11231288"}],"value":"Has a half-life of 15 minutes at 30 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15153112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}],"value":"Heterooctamer consisting of 4 large (HpdB) subunits and 4 small (HpdC) subunits. Also forms a catalytically inactive homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}],"value":"Phosphorylated on serine. Phosphorylation may trigger the formation of the active heterooctamers and thereby regulates enzyme activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15153112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16878993"}],"value":"Requires the activating protein HpdA to generate the key active site glycyl radical that is involved in catalysis"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycyl radical enzyme (GRE) family. HPAD subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11231288"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":902,"modifier":"EXACT"}},"description":"4-hydroxyphenylacetate decarboxylase glycyl radical subunit","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11231288"}],"featureId":"PRO_5000070526"},{"type":"Domain","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":774,"modifier":"EXACT"}},"description":"PFL","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00887"}]},{"type":"Domain","location":{"start":{"value":782,"modifier":"EXACT"},"end":{"value":902,"modifier":"EXACT"}},"description":"Glycine radical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00493"}]},{"type":"Active site","location":{"start":{"value":507,"modifier":"EXACT"},"end":{"value":507,"modifier":"EXACT"}},"description":"Cysteine radical intermediate","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q38HX4"}]},{"type":"Active site","location":{"start":{"value":509,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q38HX4"}]},{"type":"Binding site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:48999"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q38HX4"}],"ligand":{"name":"4-hydroxyphenylacetate","id":"ChEBI:CHEBI:48999"}},{"type":"Binding site","location":{"start":{"value":507,"modifier":"EXACT"},"end":{"value":507,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:48999"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q38HX4"}],"ligand":{"name":"4-hydroxyphenylacetate","id":"ChEBI:CHEBI:48999"}},{"type":"Binding site","location":{"start":{"value":540,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:48999"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q38HX4"}],"ligand":{"name":"4-hydroxyphenylacetate","id":"ChEBI:CHEBI:48999"}},{"type":"Binding site","location":{"start":{"value":641,"modifier":"EXACT"},"end":{"value":641,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:48999"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q38HX4"}],"ligand":{"name":"4-hydroxyphenylacetate","id":"ChEBI:CHEBI:48999"}},{"type":"Modified residue","location":{"start":{"value":877,"modifier":"EXACT"},"end":{"value":877,"modifier":"EXACT"}},"description":"Glycine radical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00493"}]}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0556","category":"PTM","name":"Organic radical"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"}],"references":[{"referenceNumber":1,"citation":{"id":"15153112","citationType":"journal article","authors":["Andrei P.I.","Pierik A.J.","Zauner S.","Andrei-Selmer L.C.","Selmer T."],"citationCrossReferences":[{"database":"PubMed","id":"15153112"},{"database":"DOI","id":"10.1111/j.1432-1033.2004.04152.x"}],"title":"Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. 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level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2374729"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3384474"}],"value":"Toxin B"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334356"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27571750"}],"value":"3.4.22.-"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Glucosyltransferase 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of a cytotoxin that targets and disrupts the colonic epithelium, inducing the host inflammatory and innate immune responses and resulting in diarrhea and pseudomembranous colitis (PubMed:20844489, PubMed:24919149). TcdB constitutes the main toxin that mediates the pathology of C.difficile infection, an opportunistic pathogen that colonizes the colon when the normal gut microbiome is disrupted (PubMed:19252482, PubMed:20844489). Compared to TcdA, TcdB is more virulent and more important for inducing the host inflammatory and innate immune responses (PubMed:19252482, PubMed:24919149). This form constitutes the precursor of the toxin: it enters into host cells and mediates autoprocessing to release the active toxin (Glucosyltransferase TcdB) into the host cytosol (PubMed:10768933, PubMed:11152463, PubMed:12941936, PubMed:17334356, PubMed:20498856). Targets colonic epithelia by binding to the frizzled receptors FZD1, FZD2 and FZD7, and enters host cells via clathrin-mediated endocytosis (PubMed:27680706). Frizzled receptors constitute the major host receptors in the colonic epithelium, but other receptors, such as CSPG4 or NECTIN3/PVRL3, have been identified (PubMed:25547119, PubMed:26038560, PubMed:27680706). Binding to carbohydrates and sulfated glycosaminoglycans on host cell surface also contribute to entry into cells (By similarity). 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 (PubMed:11152463, PubMed:12941936, PubMed:24567384). This activates the peptidase C80 domain and autocatalytic processing, releasing the N-terminal part (Glucosyltransferase TcdB), which constitutes the active part of the toxin, in the cytosol (PubMed:17334356, PubMed:27571750)"}],"commentType":"FUNCTION","molecule":"Toxin B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17901056"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24905543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24919149"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7777059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8144660"}],"value":"Active form of the toxin, which is released into the host cytosol following autoprocessing and inactivates small GTPases (PubMed:16157585, PubMed:17901056, PubMed:24905543, PubMed:24919149, PubMed:7777059, PubMed:8144660). Acts by mediating monoglucosylation of small GTPases of the Rho family (Rac1, RhoA, RhoB, RhoC, RhoG and Cdc42) in host cells at the conserved threonine residue located in the switch I region ('Thr-37/35'), using UDP-alpha-D-glucose as the sugar donor (PubMed:16157585, PubMed:17901056, PubMed:24905543, PubMed:24919149, PubMed:7777059). Monoglucosylation of host small GTPases completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption and cell death, resulting in the loss of colonic epithelial barrier function (PubMed:24919149, PubMed:7777059)"}],"commentType":"FUNCTION","molecule":"Glucosyltransferase TcdB"},{"commentType":"CATALYTIC ACTIVITY","molecule":"Glucosyltransferase TcdB","reaction":{"name":"L-threonyl-[protein] + UDP-alpha-D-glucose = 3-O-(alpha-D-glucosyl)-L-threonyl-[protein] + UDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:64684"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:16656"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:58223"},{"database":"ChEBI","id":"CHEBI:58885"},{"database":"ChEBI","id":"CHEBI:156085"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17901056"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24905543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24919149"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7777059"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:64685"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157585"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17901056"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24905543"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24919149"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7777059"}]}]},{"commentType":"COFACTOR","molecule":"Toxin B","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27571750"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31308519"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27571750"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31308519"}],"value":"Binds 1 Zn(2+) ion per subunit (PubMed:27571750, PubMed:31308519). Zn(2+) is required for autocatalytic cleavage (PubMed:27571750)."}]}},{"commentType":"COFACTOR","molecule":"Glucosyltransferase TcdB","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16054646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27089365"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28433497"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31308519"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27089365"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16054646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27089365"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28433497"}],"value":"Has higher activity with Mn(2+), but most likely uses Mg(2+) in host cells (PubMed:16054646, PubMed:28433497). Mn(2+) or Mg(2+) are required for glucosyltransferase activity (PubMed:27089365)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334356"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24821719"}],"value":"Protease activity is activated upon binding to 1D-myo-inositol hexakisphosphate (InsP6), which induces conformational reorganization (PubMed:17334356). Inhibited by bezlotoxumab, also named Zinplava, a monoclonal antibody approved by the Food and Drug Administration (FDA), which specifically targets TcdB (PubMed:24821719)"}],"commentType":"ACTIVITY REGULATION","molecule":"Toxin B"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","molecule":"Glucosyltransferase TcdB","kineticParameters":{"michaelisConstants":[{"constant":6.0,"unit":"uM","substrate":"UDP-alpha-D-glucose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157585"}]},{"constant":4.3,"unit":"uM","substrate":"UDP-alpha-D-glucose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17901056"}]},{"constant":960.0,"unit":"uM","substrate":"UDP-N-acetyl-alpha-D-glucosamine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157585"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16157585"}],"value":"kcat is 2120 h(-1) with UDP-alpha-D-glucose as substrate (PubMed:16157585). kcat is 11 h(-1) with UDP-N-acetyl-alpha-D-glucosamine as substrate (PubMed:16157585)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25547119"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26038560"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27680706"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29748286"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31233493"}],"value":"Interacts with host FZD1 (PubMed:27680706). Interacts with host FZD2; interaction promotes toxin entry into host cell and occupies the binding site for Wnt-adducted palmitoleate in FZD2, leading to prevent Wnt-binding and downstream Wnt signaling (PubMed:27680706, PubMed:29748286, PubMed:31233493). Interacts with host FZD7 (PubMed:27680706). Interacts with host CSPG4 (PubMed:25547119, PubMed:31233493). Interacts with host NECTIN3/PVRL3 (PubMed:26038560)"}],"commentType":"SUBUNIT","molecule":"Toxin B"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Toxin B","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10768933"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11152463"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12941936"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334356"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20498856"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22685398"}],"value":"Secreted from C.difficile cell into the extracellular environment via help of holin-like protein TcdE/UtxA (PubMed:22685398). Binds to the cell surface receptors via the receptor-binding region and enters the cells via clathrin-mediated endocytosis (PubMed:20498856). 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 (PubMed:10768933, PubMed:11152463, PubMed:12941936). 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C80 domain and autoprocessing, generating the Glucosyltransferase TcdB form, which is released in the host cytosol (PubMed:17334356)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22685398"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11152463"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12941936"}],"value":"Host endosome membrane","id":"SL-0394"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Glucosyltransferase TcdB","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:0000269","source":"PubMed","id":"12941936"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15632438"}],"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:0000269","source":"PubMed","id":"31308519"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"29146177"}],"value":"Consists of 4 functional domains: (1) the N-terminal GT44 domain (glucosyltransferase, 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 B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31308519"}],"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 B"},{"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 B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q46342"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25882477"}],"value":"The four-helical bundle region mediates binding to phospholipids, such as phosphatidylserine and phosphatidic acid (PubMed:25882477). This promotes localization to the inner face of the cell membrane close to small GTPases (By similarity)"}],"commentType":"DOMAIN","molecule":"Glucosyltransferase TcdB"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12941936"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334356"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27571750"}],"value":"Undergoes autocatalytic cleavage to release the N-terminal part (Glucosyltransferase TcdB), which constitutes the active part of the toxin, in the host cytosol (PubMed:12941936, PubMed:17334356, PubMed:27571750). 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C80 domain and promotes autoprocessing (PubMed:17334356)"}],"commentType":"PTM","molecule":"Toxin B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20844489"}],"value":"Cells lacking tcdB display virulence and cytotoxicity, because of the presence of TcdA (PubMed:20844489). Cells lacking both tcdA and tcdB display a strongly reduced virulence (PubMed:20844489)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the clostridial glucosylating toxin (LCGT) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15632438"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3384474"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2366,"modifier":"EXACT"}},"description":"Toxin B","featureId":"PRO_0000072636"},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":543,"modifier":"EXACT"}},"description":"Glucosyltransferase 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TcdB constitutes the main toxin that mediates the pathology of C.difficile infection, an opportunistic pathogen that colonizes the colon when the normal gut microbiome is disrupted. Compared to TcdA, TcdB is more virulent and more important for inducing the host inflammatory and innate immune responses. This form constitutes the precursor of the toxin: it enters into host cells and mediates autoprocessing to release the active toxin (Glucosyltransferase TcdB) into the host cytosol. Targets colonic epithelia by binding to the frizzled receptors FZD1, FZD2 and FZD7, and enters host cells via clathrin-mediated endocytosis. Frizzled receptors constitute the major host receptors in the colonic epithelium, but other receptors, such as CSPG4 or NECTIN3/PVRL3, have been identified (By similarity). Binding to carbohydrates and sulfated glycosaminoglycans on host cell surface also contribute to entry into cells (By similarity). 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. This activates the peptidase C80 domain and autocatalytic processing, releasing the N-terminal part (Glucosyltransferase TcdB), which constitutes the active part of the toxin, in the cytosol (By similarity)"}],"commentType":"FUNCTION","molecule":"Toxin B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"value":"Active form of the toxin, which is released into the host cytosol following autoprocessing and inactivates small GTPases. Acts by mediating monoglucosylation of small GTPases of the Rho family (Rac1, RhoA, RhoB, RhoC, RhoG and Cdc42) in host cells at the conserved threonine residue located in the switch I region ('Thr-37/35'), using UDP-alpha-D-glucose as the sugar donor. Monoglucosylation of host small GTPases completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption and cell death, resulting in the loss of colonic epithelial barrier function"}],"commentType":"FUNCTION","molecule":"Glucosyltransferase TcdB"},{"commentType":"CATALYTIC ACTIVITY","molecule":"Glucosyltransferase TcdB","reaction":{"name":"L-threonyl-[protein] + UDP-alpha-D-glucose = 3-O-(alpha-D-glucosyl)-L-threonyl-[protein] + UDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:64684"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:16656"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:58223"},{"database":"ChEBI","id":"CHEBI:58885"},{"database":"ChEBI","id":"CHEBI:156085"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:64685"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}]}]},{"commentType":"COFACTOR","molecule":"Toxin B","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"value":"Binds 1 Zn(2+) ion per subunit. Zn(2+) is required for autocatalytic cleavage."}]}},{"commentType":"COFACTOR","molecule":"Glucosyltransferase TcdB","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18177"}],"value":"Has higher activity with Mn(2+), but most likely uses Mg(2+) in host cells. 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