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Entry version 110 (07 Oct 2020)
Sequence version 2 (01 Feb 1996)
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Protein

Toxin A

Gene

tcdA

Organism
Clostridioides difficile (Peptoclostridium difficile)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 cells suface contribute to entry into cells (PubMed:1670930, PubMed:31160825, PubMed:16622409). 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).By similarity9 Publications
Active form of the toxin, which is released into the host cytosol following autoprocessing and inactivates small GTPases (PubMed:7775453, PubMed:24905543, PubMed:30622517, PubMed:22747490, PubMed:22267739). 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:7775453, PubMed:24905543, PubMed:30622517, PubMed:22747490, PubMed:22267739). 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).5 Publications

Caution

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.Curated1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Glucosyltransferase TcdA:
Mn2+3 Publications, Mg2+By similarityNote: Has higher activity with Mn2+, but most likely uses Mg2+ in host cells (By similarity). Required for glucosyltransferase activity (PubMed:22747490).By similarity1 Publication
Toxin A:
Zn2+1 PublicationNote: Binds 1 Zn2+ ion per subunit (PubMed:27571750). Zn2+ is required for autocatalytic cleavage (PubMed:27571750).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Protease activity is activated upon binding to 1D-myo-inositol hexakisphosphate (InsP6), which induces conformational reorganization.2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=43.9 µM for UDP-alpha-D-glucose (in presence of K+)1 Publication
  2. KM=36.3 µM for UDP-alpha-D-glucose (in presence of NH4+)1 Publication
  3. KM=51.1 µM for UDP-alpha-D-glucose (in presence of Na+)1 Publication
  1. Vmax=252.2 pmol/min/µg enzyme with UDP-alpha-D-glucose (in presence of K+)1 Publication
  2. Vmax=162.8 pmol/min/µg enzyme with UDP-alpha-D-glucose (in presence of NH4+)1 Publication
  3. Vmax=36.4 pmol/min/µg enzyme with UDP-alpha-D-glucose (in presence of Na+)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei138UDP-alpha-D-glucoseCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi285Magnesium or manganeseCombined sources1 Publication1
Metal bindingi287Magnesium or manganeseCombined sources3 Publications1
Metal bindingi514Magnesium or manganeseCombined sources3 Publications1
Metal bindingi544Zinc; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi545ZincCombined sources1 Publication1
Binding sitei5511D-myo-inositol hexakisphosphateCombined sources1 Publication1
Binding sitei5791D-myo-inositol hexakisphosphateCombined sources1 Publication1
Binding sitei6021D-myo-inositol hexakisphosphateCombined sources1 Publication1
Binding sitei6491D-myo-inositol hexakisphosphateCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei655For protease activityPROSITE-ProRule annotation2 Publications1
Metal bindingi655ZincCombined sources1 Publication1
Active sitei700Nucleophile; for protease activityPROSITE-ProRule annotation2 Publications1
Metal bindingi759ZincCombined sources1 Publication1
Binding sitei7661D-myo-inositol hexakisphosphateCombined sources1 Publication1
Binding sitei7771D-myo-inositol hexakisphosphateCombined sources1 Publication1
Binding sitei7941D-myo-inositol hexakisphosphateCombined sources1 Publication1
Binding sitei2540N-linked carbohydrateCombined sources1 Publication1
Binding sitei2601N-linked carbohydrate; via carbonyl oxygenCombined sources1 Publication1
Binding sitei2603N-linked carbohydrateCombined sources1 Publication1
Binding sitei2631N-linked carbohydrateCombined sources1 Publication1
Binding sitei2641N-linked carbohydrateCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionEnterotoxin, Glycosyltransferase, Hydrolase, Protease, Thiol protease, Toxin, Transferase
Biological processVirulence
LigandLipid-binding, Magnesium, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.B62, 13625
3.1.4.B4, 13625

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT44, Glycosyltransferase Family 44

MEROPS protease database

More...
MEROPSi
C80.002

Transport Classification Database

More...
TCDBi
1.C.57.1.2, the clostridial cytotoxin (cct) family

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
P16154

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Toxin A1 Publication (EC:3.4.22.-3 Publications)
Cleaved into the following chain:
Glucosyltransferase TcdACurated (EC:2.4.1.-5 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tcdA1 Publication
Synonyms:toxA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiClostridioides difficile (Peptoclostridium difficile)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1496 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaeClostridioides

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking tcdA display virulence and cytotoxity, because of the presence of TcdB (PubMed:20844489). Cells lacking both tcdA and tcdB display a strongly reduced virulence (PubMed:20844489).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi542L → A: Abolished cleavage. 1 Publication1
Mutagenesisi589D → N: Abolished protease activity and autoprocessing. 1 Publication1
Mutagenesisi590D → N: Does not affect protease activity and autoprocessing. 1 Publication1
Mutagenesisi655H → A: Abolished protease activity and autoprocessing. 2 Publications1
Mutagenesisi700C → A or S: Abolished protease activity and autoprocessing. 2 Publications1
Mutagenesisi759H → A: Abolished autoprocessing. 1 Publication1

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:9028

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3580504

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000726341 – 2710Toxin AAdd BLAST2710
ChainiPRO_00004511911 – 542Glucosyltransferase TcdA1 PublicationAdd BLAST542

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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:22267739, PubMed:19553670, PubMed:27571750). 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C80 domain and promotes autoprocessing (PubMed:17334356, PubMed:19553670).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei542 – 543Cleavage; by autolysis1 Publication2

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P16154

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with host LDLR; LDLR probably does not constitute a major receptor but may contribute to entry into cells.

1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12710
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P16154

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P16154

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini95 – 467GT44Sequence analysisAdd BLAST373
Domaini569 – 776Peptidase C80PROSITE-ProRule annotationAdd BLAST208
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1810 – 1829Cell wall-binding 1Add BLAST20
Repeati1851 – 1870Cell wall-binding 2Add BLAST20
Repeati1872 – 1891Cell wall-binding 3Add BLAST20
Repeati1923 – 1942Cell wall-binding 4Add BLAST20
Repeati1943 – 1962Cell wall-binding 5Add BLAST20
Repeati1964 – 1983Cell wall-binding 6Add BLAST20
Repeati1985 – 2004Cell wall-binding 7Add BLAST20
Repeati2006 – 2025Cell wall-binding 8Add BLAST20
Repeati2057 – 2076Cell wall-binding 9Add BLAST20
Repeati2077 – 2096Cell wall-binding 10Add BLAST20
Repeati2098 – 2117Cell wall-binding 11Add BLAST20
Repeati2119 – 2138Cell wall-binding 12Add BLAST20
Repeati2140 – 2159Cell wall-binding 13Add BLAST20
Repeati2191 – 2210Cell wall-binding 14Add BLAST20
Repeati2211 – 2230Cell wall-binding 15Add BLAST20
Repeati2232 – 2251Cell wall-binding 16Add BLAST20
Repeati2252 – 2271Cell wall-binding 17Add BLAST20
Repeati2305 – 2324Cell wall-binding 18Add BLAST20
Repeati2325 – 2344Cell wall-binding 19Add BLAST20
Repeati2346 – 2365Cell wall-binding 20Add BLAST20
Repeati2367 – 2386Cell wall-binding 21Add BLAST20
Repeati2388 – 2407Cell wall-binding 22Add BLAST20
Repeati2439 – 2458Cell wall-binding 23Add BLAST20
Repeati2459 – 2478Cell wall-binding 24Add BLAST20
Repeati2480 – 2499Cell wall-binding 25Add BLAST20
Repeati2501 – 2520Cell wall-binding 26Add BLAST20
Repeati2552 – 2571Cell wall-binding 27Add BLAST20
Repeati2572 – 2591Cell wall-binding 28Add BLAST20
Repeati2593 – 2612Cell wall-binding 29Add BLAST20
Repeati2643 – 2662Cell wall-binding 30Add BLAST20
Repeati2663 – 2682Cell wall-binding 31Add BLAST20
Repeati2685 – 2704Cell wall-binding 32Add BLAST20

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 90Four-helical bundle1 PublicationAdd BLAST90
Regioni95 – 467Glucosyltransferase region1 PublicationAdd BLAST373
Regioni100 – 102UDP-alpha-D-glucose bindingCombined sources3 Publications3
Regioni268 – 272UDP-alpha-D-glucose bindingCombined sources3 Publications5
Regioni285 – 287UDP-alpha-D-glucose bindingCombined sources3 Publications3
Regioni517 – 519UDP-alpha-D-glucose bindingCombined sources3 Publications3
Regioni543 – 801Autoprocessing region1 PublicationAdd BLAST259
Regioni753 – 7541D-myo-inositol hexakisphosphate bindingCombined sources1 Publication2
Regioni802 – 1497Translocation region1 PublicationAdd BLAST696
Regioni1832 – 2483Receptor-binding (CROPS) region1 PublicationAdd BLAST652
Regioni2547 – 2550N-linked carbohydrate bindingCombined sources1 Publication4
Regioni2567 – 2570N-linked carbohydrate bindingCombined sources1 Publication4
Regioni2569 – 2570N-linked carbohydrate bindingCombined sources1 Publication2
Regioni2638 – 2641N-linked carbohydrate bindingCombined sources1 Publication4
Regioni2658 – 2661N-linked carbohydrate bindingCombined sources1 Publication4
Regioni2660 – 2661N-linked carbohydrate bindingCombined sources1 Publication2

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.1 Publication
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.By similarity
The cell wall-binding repeats bind carbohydrates, such as Galalpha1-3Galbeta1-4GlcNAc, probably contributing to entry into cells.1 Publication1 Publication
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).By similarity1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.11050, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018337, Cell_wall/Cho-bd_repeat
IPR020974, CPD_dom
IPR038383, CPD_dom_sf
IPR029044, Nucleotide-diphossugar_trans
IPR024770, TcdA/TcdB_cat
IPR024772, TcdA/TcdB_N
IPR024769, TcdA/TcdB_pore_forming

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01473, Choline_bind_1, 5 hits
PF11713, Peptidase_C80, 1 hit
PF12919, TcdA_TcdB, 1 hit
PF12920, TcdA_TcdB_pore, 1 hit
PF12918, TcdB_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53448, SSF53448, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51771, CGT_MARTX_CPD, 1 hit
PS51170, CW, 32 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P16154-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLISKEELI KLAYSIRPRE NEYKTILTNL DEYNKLTTNN NENKYLQLKK
60 70 80 90 100
LNESIDVFMN KYKTSSRNRA LSNLKKDILK EVILIKNSNT SPVEKNLHFV
110 120 130 140 150
WIGGEVSDIA LEYIKQWADI NAEYNIKLWY DSEAFLVNTL KKAIVESSTT
160 170 180 190 200
EALQLLEEEI QNPQFDNMKF YKKRMEFIYD RQKRFINYYK SQINKPTVPT
210 220 230 240 250
IDDIIKSHLV SEYNRDETVL ESYRTNSLRK INSNHGIDIR ANSLFTEQEL
260 270 280 290 300
LNIYSQELLN RGNLAAASDI VRLLALKNFG GVYLDVDMLP GIHSDLFKTI
310 320 330 340 350
SRPSSIGLDR WEMIKLEAIM KYKKYINNYT SENFDKLDQQ LKDNFKLIIE
360 370 380 390 400
SKSEKSEIFS KLENLNVSDL EIKIAFALGS VINQALISKQ GSYLTNLVIE
410 420 430 440 450
QVKNRYQFLN QHLNPAIESD NNFTDTTKIF HDSLFNSATA ENSMFLTKIA
460 470 480 490 500
PYLQVGFMPE ARSTISLSGP GAYASAYYDF INLQENTIEK TLKASDLIEF
510 520 530 540 550
KFPENNLSQL TEQEINSLWS FDQASAKYQF EKYVRDYTGG SLSEDNGVDF
560 570 580 590 600
NKNTALDKNY LLNNKIPSNN VEEAGSKNYV HYIIQLQGDD ISYEATCNLF
610 620 630 640 650
SKNPKNSIII QRNMNESAKS YFLSDDGESI LELNKYRIPE RLKNKEKVKV
660 670 680 690 700
TFIGHGKDEF NTSEFARLSV DSLSNEISSF LDTIKLDISP KNVEVNLLGC
710 720 730 740 750
NMFSYDFNVE ETYPGKLLLS IMDKITSTLP DVNKNSITIG ANQYEVRINS
760 770 780 790 800
EGRKELLAHS GKWINKEEAI MSDLSSKEYI FFDSIDNKLK AKSKNIPGLA
810 820 830 840 850
SISEDIKTLL LDASVSPDTK FILNNLKLNI ESSIGDYIYY EKLEPVKNII
860 870 880 890 900
HNSIDDLIDE FNLLENVSDE LYELKKLNNL DEKYLISFED ISKNNSTYSV
910 920 930 940 950
RFINKSNGES VYVETEKEIF SKYSEHITKE ISTIKNSIIT DVNGNLLDNI
960 970 980 990 1000
QLDHTSQVNT LNAAFFIQSL IDYSSNKDVL NDLSTSVKVQ LYAQLFSTGL
1010 1020 1030 1040 1050
NTIYDSIQLV NLISNAVNDT INVLPTITEG IPIVSTILDG INLGAAIKEL
1060 1070 1080 1090 1100
LDEHDPLLKK ELEAKVGVLA INMSLSIAAT VASIVGIGAE VTIFLLPIAG
1110 1120 1130 1140 1150
ISAGIPSLVN NELILHDKAT SVVNYFNHLS ESKKYGPLKT EDDKILVPID
1160 1170 1180 1190 1200
DLVISEIDFN NNSIKLGTCN ILAMEGGSGH TVTGNIDHFF SSPSISSHIP
1210 1220 1230 1240 1250
SLSIYSAIGI ETENLDFSKK IMMLPNAPSR VFWWETGAVP GLRSLENDGT
1260 1270 1280 1290 1300
RLLDSIRDLY PGKFYWRFYA FFDYAITTLK PVYEDTNIKI KLDKDTRNFI
1310 1320 1330 1340 1350
MPTITTNEIR NKLSYSFDGA GGTYSLLLSS YPISTNINLS KDDLWIFNID
1360 1370 1380 1390 1400
NEVREISIEN GTIKKGKLIK DVLSKIDINK NKLIIGNQTI DFSGDIDNKD
1410 1420 1430 1440 1450
RYIFLTCELD DKISLIIEIN LVAKSYSLLL SGDKNYLISN LSNTIEKINT
1460 1470 1480 1490 1500
LGLDSKNIAY NYTDESNNKY FGAISKTSQK SIIHYKKDSK NILEFYNDST
1510 1520 1530 1540 1550
LEFNSKDFIA EDINVFMKDD INTITGKYYV DNNTDKSIDF SISLVSKNQV
1560 1570 1580 1590 1600
KVNGLYLNES VYSSYLDFVK NSDGHHNTSN FMNLFLDNIS FWKLFGFENI
1610 1620 1630 1640 1650
NFVIDKYFTL VGKTNLGYVE FICDNNKNID IYFGEWKTSS SKSTIFSGNG
1660 1670 1680 1690 1700
RNVVVEPIYN PDTGEDISTS LDFSYEPLYG IDRYINKVLI APDLYTSLIN
1710 1720 1730 1740 1750
INTNYYSNEY YPEIIVLNPN TFHKKVNINL DSSSFEYKWS TEGSDFILVR
1760 1770 1780 1790 1800
YLEESNKKIL QKIRIKGILS NTQSFNKMSI DFKDIKKLSL GYIMSNFKSF
1810 1820 1830 1840 1850
NSENELDRDH LGFKIIDNKT YYYDEDSKLV KGLININNSL FYFDPIEFNL
1860 1870 1880 1890 1900
VTGWQTINGK KYYFDINTGA ALTSYKIING KHFYFNNDGV MQLGVFKGPD
1910 1920 1930 1940 1950
GFEYFAPANT QNNNIEGQAI VYQSKFLTLN GKKYYFDNNS KAVTGWRIIN
1960 1970 1980 1990 2000
NEKYYFNPNN AIAAVGLQVI DNNKYYFNPD TAIISKGWQT VNGSRYYFDT
2010 2020 2030 2040 2050
DTAIAFNGYK TIDGKHFYFD SDCVVKIGVF STSNGFEYFA PANTYNNNIE
2060 2070 2080 2090 2100
GQAIVYQSKF LTLNGKKYYF DNNSKAVTGL QTIDSKKYYF NTNTAEAATG
2110 2120 2130 2140 2150
WQTIDGKKYY FNTNTAEAAT GWQTIDGKKY YFNTNTAIAS TGYTIINGKH
2160 2170 2180 2190 2200
FYFNTDGIMQ IGVFKGPNGF EYFAPANTDA NNIEGQAILY QNEFLTLNGK
2210 2220 2230 2240 2250
KYYFGSDSKA VTGWRIINNK KYYFNPNNAI AAIHLCTINN DKYYFSYDGI
2260 2270 2280 2290 2300
LQNGYITIER NNFYFDANNE SKMVTGVFKG PNGFEYFAPA NTHNNNIEGQ
2310 2320 2330 2340 2350
AIVYQNKFLT LNGKKYYFDN DSKAVTGWQT IDGKKYYFNL NTAEAATGWQ
2360 2370 2380 2390 2400
TIDGKKYYFN LNTAEAATGW QTIDGKKYYF NTNTFIASTG YTSINGKHFY
2410 2420 2430 2440 2450
FNTDGIMQIG VFKGPNGFEY FAPANTDANN IEGQAILYQN KFLTLNGKKY
2460 2470 2480 2490 2500
YFGSDSKAVT GLRTIDGKKY YFNTNTAVAV TGWQTINGKK YYFNTNTSIA
2510 2520 2530 2540 2550
STGYTIISGK HFYFNTDGIM QIGVFKGPDG FEYFAPANTD ANNIEGQAIR
2560 2570 2580 2590 2600
YQNRFLYLHD NIYYFGNNSK AATGWVTIDG NRYYFEPNTA MGANGYKTID
2610 2620 2630 2640 2650
NKNFYFRNGL PQIGVFKGSN GFEYFAPANT DANNIEGQAI RYQNRFLHLL
2660 2670 2680 2690 2700
GKIYYFGNNS KAVTGWQTIN GKVYYFMPDT AMAAAGGLFE IDGVIYFFGV
2710
DGVKAPGIYG
Length:2,710
Mass (Da):308,056
Last modified:February 1, 1996 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0A6E52CE84C14421
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2080L → W in AGG91568 (PubMed:24958798).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X51797 Genomic DNA Translation: CAA36094.1
M30307 Genomic DNA Translation: AAA23283.1
KC292122 Genomic DNA Translation: AGG91568.1
X92982 Genomic DNA Translation: CAA63564.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A37052

NCBI Reference Sequences

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RefSeqi
WP_009902072.1, NZ_PZRE01000002.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51797 Genomic DNA Translation: CAA36094.1
M30307 Genomic DNA Translation: AAA23283.1
KC292122 Genomic DNA Translation: AGG91568.1
X92982 Genomic DNA Translation: CAA63564.1
PIRiA37052
RefSeqiWP_009902072.1, NZ_PZRE01000002.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F6EX-ray1.85A2583-2709[»]
2G7CX-ray2.00A/B2456-2710[»]
2QJ6X-ray2.50A/B2387-2706[»]
3HO6X-ray1.60A/B543-809[»]
3SRZX-ray2.58A1-542[»]
3SS1X-ray2.20A1-542[»]
4DMVX-ray1.50A1-541[»]
4DMWX-ray2.50A1-541[»]
4NBXX-ray1.75A2573-2709[»]
4NBZX-ray1.75A/C2573-2709[»]
4R04X-ray3.26A1-1832[»]
5UMIX-ray3.23C2461-2710[»]
5UQKX-ray1.85A1-544[»]
5UQLX-ray1.97A1-544[»]
SMRiP16154
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

ChEMBLiCHEMBL3580504

Protein family/group databases

CAZyiGT44, Glycosyltransferase Family 44
MEROPSiC80.002
TCDBi1.C.57.1.2, the clostridial cytotoxin (cct) family
UniLectiniP16154

Proteomic databases

PRIDEiP16154

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P16154, 1 sequenced antibody

Enzyme and pathway databases

BRENDAi2.4.1.B62, 13625
3.1.4.B4, 13625

Miscellaneous databases

EvolutionaryTraceiP16154
PHI-baseiPHI:9028

Family and domain databases

Gene3Di3.40.50.11050, 1 hit
InterProiView protein in InterPro
IPR018337, Cell_wall/Cho-bd_repeat
IPR020974, CPD_dom
IPR038383, CPD_dom_sf
IPR029044, Nucleotide-diphossugar_trans
IPR024770, TcdA/TcdB_cat
IPR024772, TcdA/TcdB_N
IPR024769, TcdA/TcdB_pore_forming
PfamiView protein in Pfam
PF01473, Choline_bind_1, 5 hits
PF11713, Peptidase_C80, 1 hit
PF12919, TcdA_TcdB, 1 hit
PF12920, TcdA_TcdB_pore, 1 hit
PF12918, TcdB_N, 1 hit
SUPFAMiSSF53448, SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS51771, CGT_MARTX_CPD, 1 hit
PS51170, CW, 32 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTCDA_CLODI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16154
Secondary accession number(s): M4NKU2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1996
Last modified: October 7, 2020
This is version 110 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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