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Entry version 172 (18 Sep 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Botulinum neurotoxin type B

Gene

botB

Organism
Clostridium botulinum
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

Botulinum neurotoxin type B: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin B which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles (PubMed:17185412, PubMed:17167421, PubMed:17167418, PubMed:23807078). Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them (PubMed:14504267). Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway (PubMed:14504267). When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol (PubMed:3856850). Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release. Binds to host peripheral neuronal presynaptic membranes via synaptotagmins 1 and 2 (SYT1 and SYT2) (PubMed:8144634, PubMed:14504267). Toxin binds to the membrane proximal extra-cytoplasmic region of host SYT1 and SYT2 that is transiently exposed outside of cells during exocytosis; exogenous gangliosides enhance binding and subsequent uptake of toxin into host cells (PubMed:14504267, PubMed:15123599). Toxin uptake into neural cells requires stimulation (incubation with K+ to stimulate SYT protein receptor exposure); subsequently the toxin colocalizes with its receptor in host cells with a concomitant decrease in target protein (synaptobrevin-2/VAMP2) immunoreactivity (PubMed:14504267). Toxin uptake can be blocked by the appropriate synaptotagmin protein fragments and gangliosides in cell culture and in mice (PubMed:14504267, PubMed:15123599). BoNT/B is a 'coincidence detector'; it requires simultaneous binding to coreceptor GT1b and low pH to transform into a membrane-bound, oligomeric channel (PubMed:21925111, PubMed:22720883). Whole toxin only has protease activity after reduction which releases LC (PubMed:1331807, PubMed:7803399).12 Publications
Botulinum neurotoxin B light chain: Has proteolytic activity (PubMed:1331807). After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves the '76-Gln-|-Phe-77' bond of synaptobrevin-2/VAMP2, blocking neurotransmitter release (PubMed:1331807, PubMed:7803399). In vitro the LC only has protease activity after reduction (PubMed:1331807, PubMed:7803399).1 Publication1 Publication
Botulinum neurotoxin B heavy chain: Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The N-terminus of the TD wraps an extended belt around the perimeter of the LC; it does not seem to protect the active site, but might prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation (PubMed:10932256, PubMed:17167418). Has 2 coreceptors; complex gangliosides found primarily on neural tissue and host synaptotagmin-1 and -2 (SYT1 and SYT2) which bind simultaneously to adjacent but separate sites at the tip of the HC (PubMed:8144634, PubMed:17185412, PubMed:17167421, PubMed:17167418, PubMed:23807078). HC alone partially prevents uptake of whole toxin by neural cells, and delays paralysis onset by 160% (PubMed:10413679). Binding probably positions the TD for integration into the synaptic vesicle membrane (PubMed:17167418, PubMed:23807078). The HC forms channels at low pH that mediate transport of the light chain (LC) from the endocytic vesicle to the cytosol (PubMed:3856850). Binds gangliosides GD1b and GT1b (PubMed:10413679, PubMed:14731268). Gangliosides are not only a coreceptor, but also required for uptake into nerve cells (PubMed:21925111, PubMed:17167418). HC alone binds to host receptor proteins SYT1 and SYT2 (PubMed:14504267, PubMed:15123599, PubMed:17185412, PubMed:19650874). Interaction with SYT1 protein does not require SYT1 glycosylation (PubMed:19476346). The HC C-terminus (approximately residues 1079-1291) interacts with host SYT2 (PubMed:15123599, PubMed:17167421, PubMed:17167418, PubMed:23807078). Has higher affinity for SYT2 than SYT1 (PubMed:17185412, PubMed:17167421). Significantly decreases uptake and toxicity of whole BoNT/B and BoNT/G (PubMed:19650874).2 Publications11 Publications

Miscellaneous

There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes are quite frequent.
Botulism poisoning is usually food-borne, either by ingesting toxin or bacterial-contaminated food, or less frequently by inhalation poisoning. In both cases the neurotoxin binds to the apical surface of epithelial cells in the gut or airway. Toxin undergoes receptor-mediated endocytosis (using a different receptor than on target nerve cells), transcytosis across the epithelial cells and release into the general circulation. Once in the general circulation it binds to its target cells.By similarity
Types A, B and E are the most frequent cause of adult human foodborne botulism; type A is the most severe, while type E has the shortest incubation period (PubMed:1431246).1 Publication
Neurotoxin type B is released from bacteria mostly as a single chain and cleaved by host proteases into the active dichain (PubMed:4030755).1 Publication

Caution

A structure of a fragment of this protein in complex with the catalytic domain of C.botulinum neurotoxin type B (BoNT/B, botB) was reported; because of the lack of clear and continuous electron density for the VAMP2 peptide in the complex structure, the paper was retracted. One of its associated structures remains valid (PDB:1F82, light chain alone) (PubMed:10932255, PubMed:19578378).2 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

Zn2+3 PublicationsNote: Binds 1 zinc ion per subunit, to the LC (PubMed:1429690, PubMed:10932256, PubMed:17167418).3 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

Proteolysis inhibited by EDTA and captopril, and by peptides that encompass the VAMP2 cleavage site (Ala-Ser-Gln-Phe-Glu-Thr-Ser and Gln-Phe-Glu-Thr) (PubMed:1331807). Translocation of whole toxin into neurons is inhibited by toosendanin (PubMed:21925111).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

kcat is 3.96, 4.68 and 3.50 s(-1) for over-expressed human VAMP1, VAMP2 and VAMP3 respectively.1 Publication
  1. KM=19.2 µM for over-expressed human VAMP11 Publication
  2. KM=29.9 µM for over-expressed human VAMP21 Publication
  3. KM=11.6 µM for over-expressed human VAMP31 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi230Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1 Publication1
    <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 sitei231PROSITE-ProRule annotation1
    Metal bindingi234Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationCombined sources1 Publication1 Publication1
    Metal bindingi268Zinc; catalyticCombined sources1 Publication1
    <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 sitei1025Host ganglioside GT1b binding; via amide nitrogenCombined sources1

    <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 functionHydrolase, Metalloprotease, Neurotoxin, Protease, Toxin
    Biological processVirulence
    LigandLipid-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.4.24.69 1462

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-5250958 Toxicity of botulinum toxin type B (BoNT/B)

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    M27.002

    UniLectin database of carbohydrate-binding proteins

    More...
    UniLectini
    P10844

    <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:
    Botulinum neurotoxin type B
    Short name:
    BoNT/B
    Alternative name(s):
    Bontoxilysin-B
    Cleaved into the following 2 chains:
    Botulinum neurotoxin B light chain (EC:3.4.24.691 Publication)
    Short name:
    LC
    <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:botB1 Publication
    <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>OrganismiClostridium botulinum
    <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 identifieri1491 [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 lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    <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

    Botulinum neurotoxin type B :
    Chain Botulinum neurotoxin B light chain :
    Chain Botulinum neurotoxin B heavy chain :

    GO - Cellular componenti

    Keywords - Cellular componenti

    Host cell junction, Host cell membrane, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host synapse, 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 use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

    Available under the name MYOBLOC (rimabotulinumtoxinB, US WorldMeds, LLC) for the treatment of adults with cervical dystonia.

    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>Mutagenesisi1118V → D: Greatly decreased binding of heavy chain (HC) to host SYT2, whole toxin about 200-fold less toxic. Significantly decreased binding of HC to host SYT1 and SYT2 independent of gangliosides; whole toxin about 100-fold less toxic. 2 Publications1
    Mutagenesisi1183Y → R: Significantly decreased binding of heavy chain to host SYT1 and SYT2 independent of gangliosides. 1 Publication1
    Mutagenesisi1189E → L: Decreased toxicity, heavy chain has decreased binding to synaptosomes and to GT1b. 1 Publication1
    Mutagenesisi1190E → L: Greatly decreased toxicity, heavy chain has decreased binding to synaptosomes, binds less GT1b. 1 Publication1
    Mutagenesisi1191E → L: Increased binding of heavy chain to host SYT1, no effect on binding to SYT2 independent of gangliosides. 1 Publication1
    Mutagenesisi1192K → E: Greatly decreased binding of heavy chain to host SYT2, whole toxin about dramatically less toxic. Significantly decreased binding of heavy chain to host SYT1 and SYT2 independent of gangliosides; whole toxin significantly less toxic. Essentially non-toxic; when associated with L-1262. Heavy chain no longer inhibits whole-toxin uptake and toxicity. 3 Publications1
    Mutagenesisi1192K → M or Y: Decreased binding of heavy chain to host SYT1 and SYT2 independent of gangliosides. 1 Publication1
    Mutagenesisi1194F → A: Greatly decreased binding of heavy chain to host SYT2, whole toxin about 40-fold less toxic. 1 Publication1
    Mutagenesisi1196A → K: Greatly decreased binding of heavy chain to host SYT2, whole toxin about 1000-fold less toxic. 1 Publication1
    Mutagenesisi1199S → Y: Increased binding of heavy chain to host SYT2, no effect on toxicity. 1 Publication1
    Mutagenesisi1204F → A: Greatly decreased binding of heavy chain to host SYT2, whole toxin about 30-fold less toxic. 1 Publication1
    Mutagenesisi1241H → A: Decreased toxicity, heavy chain has decreased binding to synaptosomes and to GT1b. 1 Publication1
    Mutagenesisi1241H → W: Greatly decreased toxicity, heavy chain has decreased binding to synaptosomes and dramatic decrease in GT1b binding. 1 Publication1
    Mutagenesisi1260S → A: Greatly decreased toxicity, heavy chain has decreased binding to synaptosome and binds less GT1b. 1 Publication1
    Mutagenesisi1262W → L: Greatly decreased toxicity, heavy chain has decreased binding to synaptosomes, heavy chain has dramatic decrease in GT1b binding. Gangliosides no longer increase heavy chain affinity for SYT1 or SYT2; whole toxin significantly less toxic. Essentially non-toxic; when associated with E-1192. Heavy chain no longer inhibits whole-toxin uptake and toxicity. In mice without complex gangliosides no change compared to wild-type protein. 3 Publications1
    Mutagenesisi1263Y → F: Greatly decreased toxicity, heavy chain has intermediate binding to synaptosomes, binds less GT1b. 1 Publication1
    Mutagenesisi1263Y → S: Greatly decreased toxicity, heavy chain has decreased binding to synaptosomes and dramatic decrease in GT1b binding. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1075064

    Drug and drug target database

    More...
    DrugBanki
    DB02379 Beta-D-Glucose
    DB01705 Bis(5-Amidino-Benzimidazolyl)Methane
    DB13903 Equine Botulinum Neurotoxin B Immune FAB2
    DB03721 N-acetyl-alpha-neuraminic acid

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004449042 – 1291Botulinum neurotoxin type BAdd BLAST1290
    ChainiPRO_00000292152 – 441Botulinum neurotoxin B light chainAdd BLAST440
    ChainiPRO_0000029216442 – 1291Botulinum neurotoxin B heavy chainAdd BLAST850

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi437 ↔ 446Interchain (between light and heavy chains)Combined sources1 Publication2 Publications

    Keywords - PTMi

    Disulfide bond

    <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

    Heterodimer; disulfide-linked heterodimer of a light chain (LC) and a heavy chain (HC) (PubMed:3139097, PubMed:1331807). At pH 4.4 in the presence of ganglioside GT1b may form trimers (PubMed:21925111, PubMed:22720883).

    Interacts with host receptor synaptotagmin-1 (SYT1); interaction is improved in the presence of gangliosides (PubMed:8144634, PubMed:14504267, PubMed:19650874).

    Interacts with host receptor synaptotagmin-2 (SYT2) (PubMed:14504267, PubMed:15123599, PubMed:19650874, PubMed:17167421, PubMed:17167418, PubMed:23807078). SYT2 interaction and toxin uptake do not require gangliosides but are improved in their presence (PubMed:14504267, PubMed:15123599). HC interacts with a complex including at least host synaptic vesicle glycoprotein 2 (SV2) and synaptotagmin-1 (SYT1); copurification does not depend on glycosylation of either protein (PubMed:19476346).

    12 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-42782N

    Protein interaction database and analysis system

    More...
    IntActi
    P10844, 4 interactors

    Molecular INTeraction database

    More...
    MINTi
    P10844

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P10844

    <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

    11291
    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
    P10844

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P10844

    <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

    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>Regioni442 – 857Translocation domain (TD)By similarityAdd BLAST416
    Regioni481 – 532Belt; not required for channel formation1 PublicationAdd BLAST52
    Regioni858 – 1079N-terminus of receptor binding domain (N-RBD)By similarityAdd BLAST222
    Regioni1080 – 1291C-terminus of receptor binding domain (C-RBD)By similarityAdd BLAST212
    Regioni1189 – 1190Host ganglioside GT1b bindingCombined sources1 Publication1 Publication2
    Regioni1240 – 1241Galactose bindingCombined sources1 Publication1 Publication2

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1260 – 1263Host ganglioside-binding motif2 Publications1 Publication4

    <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

    Botulinum neurotoxin B light chain: Has protease activity (PubMed:1331807).1 Publication
    Botulinum neurotoxin B heavy chain: Has 3 functional domains; the translocation domain (TD) and the receptor-binding domain (RBD) which is further subdivided into N- and C-terminal domains (N-RBD and C-RBD) (PubMed:10932256). HC forms channels in bilayers at low pH (PubMed:3856850). The N-terminal belt of the TD wraps an extended belt around the perimeter of the LC; it is shorter than in BoNT/A and does not block the active site (PubMed:10932256). The belt may be a pseudosubstrate inhibitor which serves as an intramolecular chaperone for the LC prior to its translocation into the host cytosol (PubMed:17907800).1 Publication2 Publications

    <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

    Belongs to the peptidase M27 family.Curated

    Keywords - Domaini

    Transmembrane

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.20.1120.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000395 Bot/tetX_LC
    IPR036248 Clostridium_toxin_transloc
    IPR013320 ConA-like_dom_sf
    IPR011065 Kunitz_inhibitor_STI-like_sf
    IPR013104 Toxin_rcpt-bd_C
    IPR012928 Toxin_rcpt-bd_N
    IPR012500 Toxin_trans

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01742 Peptidase_M27, 1 hit
    PF07951 Toxin_R_bind_C, 1 hit
    PF07953 Toxin_R_bind_N, 1 hit
    PF07952 Toxin_trans, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00760 BONTOXILYSIN

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF49899 SSF49899, 1 hit
    SSF50386 SSF50386, 1 hit
    SSF58091 SSF58091, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00142 ZINC_PROTEASE, 1 hit

    <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.

    P10844-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPVTINNFNY NDPIDNNNII MMEPPFARGT GRYYKAFKIT DRIWIIPERY
    60 70 80 90 100
    TFGYKPEDFN KSSGIFNRDV CEYYDPDYLN TNDKKNIFLQ TMIKLFNRIK
    110 120 130 140 150
    SKPLGEKLLE MIINGIPYLG DRRVPLEEFN TNIASVTVNK LISNPGEVER
    160 170 180 190 200
    KKGIFANLII FGPGPVLNEN ETIDIGIQNH FASREGFGGI MQMKFCPEYV
    210 220 230 240 250
    SVFNNVQENK GASIFNRRGY FSDPALILMH ELIHVLHGLY GIKVDDLPIV
    260 270 280 290 300
    PNEKKFFMQS TDAIQAEELY TFGGQDPSII TPSTDKSIYD KVLQNFRGIV
    310 320 330 340 350
    DRLNKVLVCI SDPNININIY KNKFKDKYKF VEDSEGKYSI DVESFDKLYK
    360 370 380 390 400
    SLMFGFTETN IAENYKIKTR ASYFSDSLPP VKIKNLLDNE IYTIEEGFNI
    410 420 430 440 450
    SDKDMEKEYR GQNKAINKQA YEEISKEHLA VYKIQMCKSV KAPGICIDVD
    460 470 480 490 500
    NEDLFFIADK NSFSDDLSKN ERIEYNTQSN YIENDFPINE LILDTDLISK
    510 520 530 540 550
    IELPSENTES LTDFNVDVPV YEKQPAIKKI FTDENTIFQY LYSQTFPLDI
    560 570 580 590 600
    RDISLTSSFD DALLFSNKVY SFFSMDYIKT ANKVVEAGLF AGWVKQIVND
    610 620 630 640 650
    FVIEANKSNT MDKIADISLI VPYIGLALNV GNETAKGNFE NAFEIAGASI
    660 670 680 690 700
    LLEFIPELLI PVVGAFLLES YIDNKNKIIK TIDNALTKRN EKWSDMYGLI
    710 720 730 740 750
    VAQWLSTVNT QFYTIKEGMY KALNYQAQAL EEIIKYRYNI YSEKEKSNIN
    760 770 780 790 800
    IDFNDINSKL NEGINQAIDN INNFINGCSV SYLMKKMIPL AVEKLLDFDN
    810 820 830 840 850
    TLKKNLLNYI DENKLYLIGS AEYEKSKVNK YLKTIMPFDL SIYTNDTILI
    860 870 880 890 900
    EMFNKYNSEI LNNIILNLRY KDNNLIDLSG YGAKVEVYDG VELNDKNQFK
    910 920 930 940 950
    LTSSANSKIR VTQNQNIIFN SVFLDFSVSF WIRIPKYKND GIQNYIHNEY
    960 970 980 990 1000
    TIINCMKNNS GWKISIRGNR IIWTLIDING KTKSVFFEYN IREDISEYIN
    1010 1020 1030 1040 1050
    RWFFVTITNN LNNAKIYING KLESNTDIKD IREVIANGEI IFKLDGDIDR
    1060 1070 1080 1090 1100
    TQFIWMKYFS IFNTELSQSN IEERYKIQSY SEYLKDFWGN PLMYNKEYYM
    1110 1120 1130 1140 1150
    FNAGNKNSYI KLKKDSPVGE ILTRSKYNQN SKYINYRDLY IGEKFIIRRK
    1160 1170 1180 1190 1200
    SNSQSINDDI VRKEDYIYLD FFNLNQEWRV YTYKYFKKEE EKLFLAPISD
    1210 1220 1230 1240 1250
    SDEFYNTIQI KEYDEQPTYS CQLLFKKDEE STDEIGLIGI HRFYESGIVF
    1260 1270 1280 1290
    EEYKDYFCIS KWYLKEVKRK PYNLKLGCNW QFIPKDEGWT E
    Length:1,291
    Mass (Da):150,803
    Last modified:January 23, 2007 - v3
    <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:i921DE5C518140DBD
    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 conflicti30T → M AA sequence (PubMed:3139097).Curated1
    Sequence conflicti218R → G in CAA77991 (Ref. 2) Curated1
    Sequence conflicti225A → S in CAA77991 (Ref. 2) Curated1
    Sequence conflicti464S → R AA sequence (PubMed:3139097).Curated1

    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
    M81186 Genomic DNA Translation: AAA23211.1
    Z11934 Genomic DNA Translation: CAA77991.1
    X70817 Genomic DNA Translation: CAA50148.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A48940

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    BotDB - A Database Resource for Clostridial Neurotoxins

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M81186 Genomic DNA Translation: AAA23211.1
    Z11934 Genomic DNA Translation: CAA77991.1
    X70817 Genomic DNA Translation: CAA50148.1
    PIRiA48940

    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
    1EPWX-ray1.90A2-1291[»]
    1F31X-ray2.60A2-1291[»]
    1F82X-ray2.20A2-425[»]
    1G9AX-ray2.10A2-1291[»]
    1G9BX-ray2.00A2-1291[»]
    1G9CX-ray2.35A2-1291[»]
    1G9DX-ray2.20A2-1291[»]
    1I1EX-ray2.50A2-1291[»]
    1S0BX-ray2.00A2-1291[»]
    1S0CX-ray2.20A2-1291[»]
    1S0DX-ray2.20A2-1291[»]
    1S0EX-ray1.90A2-1291[»]
    1S0FX-ray2.30A2-1291[»]
    1S0GX-ray2.60A2-1291[»]
    1Z0HX-ray2.00A/B854-1291[»]
    2ETFX-ray2.29A/B1-441[»]
    2NM1X-ray2.15A858-1291[»]
    2NP0X-ray2.62A2-1291[»]
    2XHLX-ray2.80A1-437[»]
    B446-858[»]
    3ZUQX-ray2.70A1-437[»]
    A446-858[»]
    4KBBX-ray2.30A/B857-1291[»]
    5VIDX-ray2.75A/B/C/D/E859-1291[»]
    5VMRX-ray1.95A/B859-1291[»]
    6G5FX-ray2.50A/B1-1291[»]
    6G5GX-ray2.00A/B1-1291[»]
    6G5KX-ray2.00A/B857-1291[»]
    SMRiP10844
    ModBaseiSearch...

    Protein-protein interaction databases

    DIPiDIP-42782N
    IntActiP10844, 4 interactors
    MINTiP10844

    Chemistry databases

    BindingDBiP10844
    ChEMBLiCHEMBL1075064
    DrugBankiDB02379 Beta-D-Glucose
    DB01705 Bis(5-Amidino-Benzimidazolyl)Methane
    DB13903 Equine Botulinum Neurotoxin B Immune FAB2
    DB03721 N-acetyl-alpha-neuraminic acid

    Protein family/group databases

    MEROPSiM27.002
    UniLectiniP10844

    Protocols and materials databases

    ABCD curated depository of sequenced antibodies

    More...
    ABCDi
    P10844
    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.4.24.69 1462
    ReactomeiR-HSA-5250958 Toxicity of botulinum toxin type B (BoNT/B)

    Miscellaneous databases

    EvolutionaryTraceiP10844

    Family and domain databases

    Gene3Di1.20.1120.10, 1 hit
    InterProiView protein in InterPro
    IPR000395 Bot/tetX_LC
    IPR036248 Clostridium_toxin_transloc
    IPR013320 ConA-like_dom_sf
    IPR011065 Kunitz_inhibitor_STI-like_sf
    IPR013104 Toxin_rcpt-bd_C
    IPR012928 Toxin_rcpt-bd_N
    IPR012500 Toxin_trans
    PfamiView protein in Pfam
    PF01742 Peptidase_M27, 1 hit
    PF07951 Toxin_R_bind_C, 1 hit
    PF07953 Toxin_R_bind_N, 1 hit
    PF07952 Toxin_trans, 1 hit
    PRINTSiPR00760 BONTOXILYSIN
    SUPFAMiSSF49899 SSF49899, 1 hit
    SSF50386 SSF50386, 1 hit
    SSF58091 SSF58091, 1 hit
    PROSITEiView protein in PROSITE
    PS00142 ZINC_PROTEASE, 1 hit

    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 nameiBXB_CLOBO
    <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: P10844
    Secondary accession number(s): P10843
    <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: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: September 18, 2019
    This is version 172 of the entry and version 3 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, Direct protein sequencing, Pharmaceutical

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Peptidase families
      Classification of peptidase families and list of entries
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