Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 94 (29 Sep 2021)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Add a publicationFeedback
Protein

Cytotoxin-L

Gene

tcsL

Organism
Paeniclostridium sordellii (Clostridium sordellii)
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 the vascular endothelium, inducing an anti-inflammatory effect and resulting in lethal toxic shock syndrome (PubMed:19527792, PubMed:24919149, PubMed:29146177).

TcsL constitutes the main toxin that mediates the pathology of P.sordellii infection, an anaerobic Gram-positive bacterium found in soil and in the gastrointestinal and vaginal tracts of animals and humans; although the majority of carriers are asymptomatic, pathogenic P.sordellii infections arise rapidly and are highly lethal (PubMed:29146177).

This form constitutes the precursor of the toxin: it enters into host cells and mediates autoprocessing to release the active toxin (Glucosyltransferase TcsL) into the host cytosol (PubMed:32302524, PubMed:17334356, PubMed:27303685).

Targets vascular endothelium by binding to the semaphorin proteins SEMA6A and SEMA6B, and enters host cells via clathrin-mediated endocytosis (PubMed:32302524).

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 TcsL), which constitutes the active part of the toxin, in the cytosol (PubMed:17334356, PubMed:27303685).

1 PublicationBy similarity5 Publications

Active form of the toxin, which is released into the host cytosol following autoprocessing and inactivates small GTPases (PubMed:8626575, PubMed:8626586, PubMed:9632667, PubMed:17901056, PubMed:19744486, PubMed:24905543, PubMed:24919149, PubMed:27303685, PubMed:27023605, PubMed:30622517).

Acts by mediating monoglucosylation of small GTPases of the Ras (H-Ras/HRAS, K-Ras/KRAS, N-Ras/NRAS and Ral/RALA) family 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:8858106, PubMed:8626575, PubMed:8626586, PubMed:9632667, PubMed:17901056, PubMed:19744486, PubMed:24905543, PubMed:24919149, PubMed:27023605, PubMed:30622517).

Also able to catalyze monoglucosylation of some members of the Rho family (Rac1 and Rap2A), but with less efficiency than with Ras proteins (PubMed:8626586, PubMed:9632667, PubMed:19744486, PubMed:24905543).

Monoglucosylation of host small GTPases completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form and leading to apoptosis (PubMed:8626586, PubMed:9632667, PubMed:17910886).

Induces an anti-inflammatory effect, mainly by inactivating Ras proteins which results in blockage of the cell cycle and killing of immune cells (PubMed:17910886, PubMed:24919149).

The absence or moderate local inflammatory response allows C.sordellii spreading in deep tissues, production of toxin which is released in the general circulation and causes a toxic shock syndrome (PubMed:24919149, PubMed:29146177).

1 Publication12 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Cytotoxin-L:
Zn2+By similarityNote: Binds 1 Zn2+ ion per subunit. Zn2+ is required for autocatalytic cleavage.By similarity
Glucosyltransferase TcsL:
Mn2+2 Publications, Mg2+1 PublicationNote: Has higher activity with Mn2+, but most likely uses Mg2+ in host cells (PubMed:27089365). Mn2+ or Mg2+ are required for glucosyltransferase activity (PubMed:8626575, PubMed:27089365).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei139UDP-alpha-D-glucoseCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi288Magnesium or manganeseCombined sources1 Publication1
Metal bindingi515Magnesium or manganeseCombined sources1 Publication1
Metal bindingi518Magnesium or manganeseCombined sources2 Publications1
Metal bindingi545Zinc; via carbonyl oxygenBy similarity1
Metal bindingi546ZincBy similarity1
Binding sitei5771D-myo-inositol hexakisphosphateBy similarity1
Binding sitei6001D-myo-inositol hexakisphosphateBy similarity1
Binding sitei6471D-myo-inositol hexakisphosphateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei653For protease activityPROSITE-ProRule annotation1
Metal bindingi653ZincBy similarity1
Active sitei698Nucleophile; for protease activityPROSITE-ProRule annotation1 Publication1
Metal bindingi757ZincBy similarity1
Binding sitei7641D-myo-inositol hexakisphosphateBy similarity1
Binding sitei7751D-myo-inositol hexakisphosphateBy similarity1
Binding sitei7921D-myo-inositol hexakisphosphateBy similarity1

<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 functionGlycosyltransferase, 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, 1514

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT44, Glycosyltransferase Family 44

Transport Classification Database

More...
TCDBi
1.C.57.1.3, the clostridial cytotoxin (cct) family

<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_and_taxonomy_section">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:
Cytotoxin-L1 Publication (EC:3.4.22.-1 Publication)
Alternative name(s):
Lethal toxin2 Publications
Short name:
LT2 Publications
Cleaved into the following chain:
Glucosyltransferase TcsLCurated (EC:2.4.1.-7 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:tcsL2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiPaeniclostridium sordellii (Clostridium sordellii)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri1505 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaFirmicutesClostridiaEubacterialesPeptostreptococcaceaePaeniclostridium

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi10Q → A: Does not affect phospholipid-binding and cytotoxicity. 1 Publication1
Mutagenesisi11K → I: Slightly reduced phospholipid-binding and impaired cytotoxicity. 1 Publication1
Mutagenesisi14Y → A: Strongly reduced phospholipid-binding without affecting cytotoxicity. 1 Publication1
Mutagenesisi15V → S: Strongly reduced phospholipid-binding and impaired cytotoxicity. 1 Publication1
Mutagenesisi16K → I: Slightly reduced phospholipid-binding. 1 Publication1
Mutagenesisi17 – 18FR → NA: Impaired localization to host cell membrane, leading to impaired cytotoxicity. 1 Publication2
Mutagenesisi17F → K: Strongly reduced phospholipid-binding and impaired cytotoxicity. 1 Publication1
Mutagenesisi18R → P: Strongly reduced phospholipid-binding and impaired cytotoxicity. 1 Publication1
Mutagenesisi20Q → A: Slightly reduced phospholipid-binding without affecting cytotoxicity. 1 Publication1
Mutagenesisi38S → A: Does not affect phospholipid-binding and cytotoxicity. 1 Publication1
Mutagenesisi68R → A: Strongly reduced phospholipid-binding without affecting cytotoxicity. 1 Publication1
Mutagenesisi78Y → A: Does not affect phospholipid-binding and cytotoxicity. 1 Publication1
Mutagenesisi286 – 288DVD → NVN: Abolished glucosyltransferase activity without affecting localization to the host cell membrane. 3 Publications3
Mutagenesisi698C → A: Abolished autoprocessing, leading to impaired cytotoxicity. 1 Publication1

<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_00004511971 – 2364Cytotoxin-LAdd BLAST2364
ChainiPRO_00004511981 – 543Glucosyltransferase TcsLBy similarityAdd BLAST543

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 TcsL), which constitutes the active part of the toxin, in the host cytosol (PubMed:17334356, PubMed:27303685). 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C80 domain and promotes autoprocessing (PubMed:17334356).2 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>Sitei543 – 544Cleavage; by autolysisBy similarity2

Keywords - PTMi

Autocatalytic cleavage

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homomultimer; forms an inactive homomultimer at pH 8, which dissociates at pH 4, leading to cytotoxicity (By similarity).

Interacts with host SEMA6A; interaction promotes toxin entry into host cell (PubMed:32302524).

Interacts with host SEMA6B; interaction promotes toxin entry into host cell (PubMed:32302524).

By similarity1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q46342, 4 interactors

Molecular INTeraction database

More...
MINTi
Q46342

<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

12364
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
Q46342

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
Q46342

<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_and_domains_section">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>Domaini96 – 468GT44Sequence analysisAdd BLAST373
Domaini567 – 774Peptidase 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>Repeati1813 – 1832Cell wall-binding 1PROSITE-ProRule annotationAdd BLAST20
Repeati1833 – 1852Cell wall-binding 2PROSITE-ProRule annotationAdd BLAST20
Repeati1854 – 1873Cell wall-binding 3PROSITE-ProRule annotationAdd BLAST20
Repeati1876 – 1895Cell wall-binding 4PROSITE-ProRule annotationAdd BLAST20
Repeati1926 – 1945Cell wall-binding 5PROSITE-ProRule annotationAdd BLAST20
Repeati1946 – 1965Cell wall-binding 6PROSITE-ProRule annotationAdd BLAST20
Repeati1967 – 1986Cell wall-binding 7PROSITE-ProRule annotationAdd BLAST20
Repeati1987 – 2006Cell wall-binding 8PROSITE-ProRule annotationAdd BLAST20
Repeati2007 – 2026Cell wall-binding 9PROSITE-ProRule annotationAdd BLAST20
Repeati2057 – 2076Cell wall-binding 10PROSITE-ProRule annotationAdd BLAST20
Repeati2077 – 2097Cell wall-binding 11PROSITE-ProRule annotationAdd BLAST21
Repeati2099 – 2118Cell wall-binding 12PROSITE-ProRule annotationAdd BLAST20
Repeati2119 – 2138Cell wall-binding 13PROSITE-ProRule annotationAdd BLAST20
Repeati2139 – 2158Cell wall-binding 14PROSITE-ProRule annotationAdd BLAST20
Repeati2209 – 2224Cell wall-binding 15PROSITE-ProRule annotationAdd BLAST16
Repeati2227 – 2249Cell wall-binding 16PROSITE-ProRule annotationAdd BLAST23
Repeati2250 – 2269Cell wall-binding 17PROSITE-ProRule annotationAdd BLAST20
Repeati2270 – 2289Cell wall-binding 18PROSITE-ProRule annotationAdd BLAST20
Repeati2320 – 2339Cell wall-binding 19PROSITE-ProRule annotationAdd BLAST20
Repeati2340 – 2359Cell wall-binding 20PROSITE-ProRule annotationAdd 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 – 91Four-helical bundle1 PublicationAdd BLAST91
Regioni96 – 468Glucosyltransferase region1 PublicationAdd BLAST373
Regioni101 – 103UDP-alpha-D-glucose bindingCombined sources2 Publications3
Regioni265 – 270UDP-alpha-D-glucose bindingCombined sources2 Publications6
Regioni286 – 288UDP-alpha-D-glucose bindingCombined sources2 Publications3
Regioni518 – 520UDP-alpha-D-glucose bindingCombined sources1 Publication3
Regioni544 – 799Autoprocessing region1 PublicationAdd BLAST256
Regioni800 – 1500Translocation region1 PublicationAdd BLAST701
Regioni1433 – 1438Interaction with host SEMA6A and SEMA6BBy similarity6
Regioni1466 – 1471Interaction with host SEMA6A and SEMA6BBy similarity6
Regioni1484 – 1495Interaction with host SEMA6A and SEMA6BBy similarityAdd BLAST12
Regioni1504 – 1511Interaction with host SEMA6A and SEMA6BBy similarity8
Regioni1596 – 1601Interaction with host SEMA6A and SEMA6BBy similarity6
Regioni1835 – 2364Receptor-binding (CROPS) region1 PublicationAdd BLAST530

<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, probably contributing to entry into cells.By similarity
The four-helical bundle region mediates binding to phospholipids, such as phosphatidylserine and phosphatidic acid (PubMed:27023605). This promotes localization to the inner face of the cell membrane close to small GTPases (PubMed:27023605).1 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
PF19127, Choline_bind_3, 1 hit
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, 20 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q46342-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLVNKAQLQ KMVYVKFRIQ EDEYVAILNA LEEYHNMSES SVVEKYLKLK
60 70 80 90 100
DINNLTDNYL NTYKKSGRNK ALKKFKEYLT MEVLELKNNS LTPVEKNLHF
110 120 130 140 150
IWIGGQINDT AINYINQWKD VNSDYTVKVF YDSNAFLINT LKKTIVESAT
160 170 180 190 200
NNTLESFREN LNDPEFDYNK FYRKRMEIIY DKQKHFIDYY KSQIEENPEF
210 220 230 240 250
IIDNIIKTYL SNEYSKDLEA LNKYIEESLN KITANNGNDI RNLEKFADED
260 270 280 290 300
LVRLYNQELV ERWNLAAASD ILRISMLKED GGVYLDVDIL PGIQPDLFKS
310 320 330 340 350
INKPDSITNT SWEMIKLEAI MKYKEYIPGY TSKNFDMLDE EVQRSFESAL
360 370 380 390 400
SSKSDKSEIF LPLDDIKVSP LEVKIAFANN SVINQALISL KDSYCSDLVI
410 420 430 440 450
NQIKNRYKIL NDNLNPSINE GTDFNTTMKI FSDKLASISN EDNMMFMIKI
460 470 480 490 500
TNYLKVGFAP DVRSTINLSG PGVYTGAYQD LLMFKDNSTN IHLLEPELRN
510 520 530 540 550
FEFPKTKISQ LTEQEITSLW SFNQARAKSQ FEEYKKGYFE GALGEDDNLD
560 570 580 590 600
FAQNTVLDKD YVSKKILSSM KTRNKEYIHY IVQLQGDKIS YEASCNLFSK
610 620 630 640 650
DPYSSILYQK NIEGSETAYY YYVADAEIKE IDKYRIPYQI SNKRNIKLTF
660 670 680 690 700
IGHGKSEFNT DTFANLDVDS LSSEIETILN LAKADISPKY IEINLLGCNM
710 720 730 740 750
FSYSISAEET YPGKLLLKIK DRVSELMPSI SQDSITVSAN QYEVRINEEG
760 770 780 790 800
KREILDHSGK WINKEESIIK DISSKEYISF NPKENKIIVK SKYLHELSTL
810 820 830 840 850
LQEIRNNANS SDIDLEKKVM LTECEINVAS NIDRQIVEGR IEEAKNLTSD
860 870 880 890 900
SINYIKNEFK LIESISDSLY DLKHQNGLDD SHFISFEDIS KTENGFRIRF
910 920 930 940 950
INKETGNSIF IETEKEIFSE YATHISKEIS NIKDTIFDNV NGKLVKKVNL
960 970 980 990 1000
DAAHEVNTLN SAFFIQSLIE YNTTKESLSN LSVAMKVQVY AQLFSTGLNT
1010 1020 1030 1040 1050
ITDASKVVEL VSTALDETID LLPTLSEGLP IIATIIDGVS LGAAIKELSE
1060 1070 1080 1090 1100
TNDPLLRQEI EAKIGIMAVN LTAASTAIVT SALGIASGFS ILLVPLAGIS
1110 1120 1130 1140 1150
AGIPSLVNNE LILQDKATKV IDYFKHISLA ETEGAFTLLD DKIIMPQDDL
1160 1170 1180 1190 1200
VLSEIDFNNN SITLGKCEIW RAEGGSGHTL TDDIDHFFSS PSITYRKPWL
1210 1220 1230 1240 1250
SIYDVLNIKK EKIDFSKDLM VLPNAPNRVF GYEMGWTPGF RSLDNDGTKL
1260 1270 1280 1290 1300
LDRIRDHYEG QFYWRYFAFI ADALITKLKP RYEDTNVRIN LDGNTRSFIV
1310 1320 1330 1340 1350
PVITTEQIRK NLSYSFYGSG GSYSLSLSPY NMNIDLNLVE NDTWVIDVDN
1360 1370 1380 1390 1400
VVKNITIESD EIQKGELIEN ILSKLNIEDN KIILNNHTIN FYGDINESNR
1410 1420 1430 1440 1450
FISLTFSILE DINIIIEIDL VSKSYKILLS GNCMKLIENS SDIQQKIDHI
1460 1470 1480 1490 1500
GFNGEHQKYI PYSYIDNETK YNGFIDYSKK EGLFTAEFSN ESIIRNIYMP
1510 1520 1530 1540 1550
DSNNLFIYSS KDLKDIRIIN KGDVKLLIGN YFKDDMKVSL SFTIEDTNTI
1560 1570 1580 1590 1600
KLNGVYLDEN GVAQILKFMN NAKSALNTSN SLMNFLESIN IKNIFYNNLD
1610 1620 1630 1640 1650
PNIEFILDTN FIISGSNSIG QFELICDKDK NIQPYFINFK IKETSYTLYV
1660 1670 1680 1690 1700
GNRQNLIVEP SYHLDDSGNI SSTVINFSQK YLYGIDRYVN KVIIAPNLYT
1710 1720 1730 1740 1750
DEINITPVYK PNYICPEVII LDANYINEKI NVNINDLSIR YVWDNDGSDL
1760 1770 1780 1790 1800
ILIANSEEDN QPQVKIRFVN VFKSDTAADK LSFNFSDKQD VSVSKIISTF
1810 1820 1830 1840 1850
SLAAYSDGFF DYEFGLVSLD NDYFYINSFG NMVSGLIYIN DSLYYFKPPK
1860 1870 1880 1890 1900
NNLITGFTTI DGNKYYFDPT KSGAASIGEI TIDGKDYYFN KQGILQVGVI
1910 1920 1930 1940 1950
NTSDGLKYFA PAGTLDENLE GESVNFIGKL NIDGKIYYFE DNYRAAVEWK
1960 1970 1980 1990 2000
LLDDETYYFN PKTGEALKGL HQIGDNKYYF DDNGIMQTGF ITINDKVFYF
2010 2020 2030 2040 2050
NNDGVMQVGY IEVNGKYFYF GKNGERQLGV FNTPDGFKFF GPKDDDLGTE
2060 2070 2080 2090 2100
EGELTLYNGI LNFNGKIYFF DISNTAVVGW GTLDDGSTYY FDDNRAEACI
2110 2120 2130 2140 2150
GLTVINDCKY YFDDNGIRQL GFITINDNIF YFSESGKIEL GYQNINGNYF
2160 2170 2180 2190 2200
YIDESGLVLI GVFDTPDGYK YFAPLNTVND NIYGQAVKYS GLVRVNEDVY
2210 2220 2230 2240 2250
YFGETYKIET GWIENETDKY YFDPETKKAY KGINVVDDIK YYFDENGIMR
2260 2270 2280 2290 2300
TGLISFENNN YYFNEDGKMQ FGYLNIKDKM FYFGKDGKMQ IGVFNTPDGF
2310 2320 2330 2340 2350
KYFAHQNTLD ENFEGESINY TGWLDLDGKR YYFTDEYIAA TGSLTIDGYN
2360
YYFDPDTAEL VVSE
Length:2,364
Mass (Da):270,580
Last modified:November 1, 1996 - v1
<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:iEAD8A4467A89BDBB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X82638 Genomic DNA Translation: CAA57959.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I40884

<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
X82638 Genomic DNA Translation: CAA57959.1
PIRiI40884

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VKDX-ray2.53A/B/C1-546[»]
2VKHX-ray2.30A/B/C1-546[»]
2VL8X-ray2.31A/B/C1-546[»]
SMRiQ46342
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiQ46342, 4 interactors
MINTiQ46342

Protein family/group databases

CAZyiGT44, Glycosyltransferase Family 44
TCDBi1.C.57.1.3, the clostridial cytotoxin (cct) family

Enzyme and pathway databases

BRENDAi2.4.1.B62, 1514

Miscellaneous databases

EvolutionaryTraceiQ46342

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
PF19127, Choline_bind_3, 1 hit
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, 20 hits

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 nameiTCSL1_PAESO
<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: Q46342
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 7, 2020
Last sequence update: November 1, 1996
Last modified: September 29, 2021
This is version 94 of the entry and version 1 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again