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Entry version 152 (11 Dec 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Botulinum neurotoxin type A2

Gene

botA

Organism
Clostridium botulinum (strain Kyoto / Type A2)
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 toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin A2 which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. 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. 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 (By similarity).By similarity
Has proteolytic activity. After translocation into the eukaryotic host cytosol, LC hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP25, blocking neurotransmitter release (PubMed:16846233).1 Publication
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 RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and the receptor protein SV2 in close proximity on host synaptic vesicles (PubMed:28252640, PubMed:29649119). The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn2+ in the active site; it may also prevent premature LC dissociation from the translocation channel and to protect toxin prior to translocation (By similarity). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (By similarity).By similarity2 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

<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

  • Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.1 Publication EC:3.4.24.69

<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+2 PublicationsNote: Binds 1 zinc ion per subunit (PubMed:15107500, PubMed:16846233).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 of LC inhibited by arginine hydroxamate.1 Publication

<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 0.13 sec(-1), for botulinum neurotoxin A2 light chain.1 Publication
  1. KM=14.1 µM for SNAP25 fragment (146-206) with isolated botulinum neurotoxin A2 light chain1 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 bindingi223Zinc; via tele nitrogen; catalyticCombined sources2 Publications1
    <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 sitei224PROSITE-ProRule annotation1
    Metal bindingi227Zinc; via tele nitrogen; catalyticCombined sources2 Publications1
    Metal bindingi262Zinc; catalyticCombined sources2 Publications1
    <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>Sitei366Transition state stabilizer1 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 functionHydrolase, Metalloprotease, Neurotoxin, Protease, Toxin
    Biological processVirulence
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    CBOT536232:G1GVA-850-MONOMER

    <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 A2
    Short name:
    BoNT/A
    Alternative name(s):
    Bontoxilysin-A1 Publication
    Short name:
    BOTOX
    Cleaved into the following 2 chains:
    Botulinum neurotoxin A2 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:botA1 Publication
    Synonyms:atx, bna, bonT1 Publication
    Ordered Locus Names:CLM_0897Imported
    <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 (strain Kyoto / Type A2)
    <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 identifieri536232 [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 subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000001374 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <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

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei627 – 647HelicalSequence analysisAdd BLAST21
    Transmembranei656 – 676HelicalSequence analysisAdd BLAST21

    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

    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>Mutagenesisi370D → A: 600-fold decrease in cleavage rate of SNAP25 by light chain. 1 Publication1
    Mutagenesisi1156E → R: Decreased binding to human SV2C extracellular loop 4 fragment. 1 Publication1

    Protein family/group databases

    Allergome; a platform for allergen knowledge

    More...
    Allergomei
    12104 Clo bo Toxin

    <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 methionineiRemovedBy similarity
    <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_00004449182 – 1296Botulinum neurotoxin type A2Add BLAST1295
    ChainiPRO_00000292132 – 448Botulinum neurotoxin A2 light chainAdd BLAST447
    ChainiPRO_0000029214449 – 1296Botulinum neurotoxin A2 heavy chainAdd BLAST848

    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 bondi430 ↔ 454Interchain (between light and heavy chains)By similarity
    Disulfide bondi1235 ↔ 1280Combined sources1 Publication

    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).

    Interacts with host synaptic vesicle glycoprotein 2C (SV2C) which serves as a coreceptor (PubMed:28252640). Also binds host receptor proteins SV2A and SV2B; glycosylation of host protein greatly improves the interaction (PubMed:29649119).

    2 Publications

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-437N

    STRING: functional protein association networks

    More...
    STRINGi
    536232.CLM_0897

    <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

    11296
    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
    Q45894

    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
    Q45894

    <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>Regioni449 – 870Translocation domain (TD)By similarityAdd BLAST422
    Regioni492 – 545Belt; not required for channel formationBy similarityAdd BLAST54
    Regioni871 – 1092N-terminus of receptor binding domain (N-RBD)By similarity1 PublicationAdd BLAST222
    Regioni1093 – 1296C-terminus of receptor binding domain (C-RBD)By similarity1 PublicationAdd BLAST204

    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>Motifi1264 – 1267Host ganglioside-binding motifBy similarity4

    <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

    Has protease activity.1 Publication
    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:28252640, PubMed:29649119). The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn2+ in the active site and may be a pseudosubstrate inhibitor which serves as an intramolecular chaperone for the LC prior to its translocation into the host cytosol. The RBD binds transiently exposed coreceptors on the host presynaptic cell membrane (PubMed:28252640).By similarity2 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, Transmembrane helix

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000234384

    KEGG Orthology (KO)

    More...
    KOi
    K06011

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DEGYNKA

    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

    <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.

    Q45894-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPFVNKQFNY KDPVNGVDIA YIKIPNAGQM QPVKAFKIHN KIWVIPERDT
    60 70 80 90 100
    FTNPEEGDLN PPPEAKQVPV SYYDSTYLST DNEKDNYLKG VTKLFERIYS
    110 120 130 140 150
    TDLGRMLLTS IVRGIPFWGG STIDTELKVI DTNCINVIQP DGSYRSEELN
    160 170 180 190 200
    LVIIGPSADI IQFECKSFGH DVLNLTRNGY GSTQYIRFSP DFTFGFEESL
    210 220 230 240 250
    EVDTNPLLGA GKFATDPAVT LAHELIHAEH RLYGIAINPN RVFKVNTNAY
    260 270 280 290 300
    YEMSGLEVSF EELRTFGGHD AKFIDSLQEN EFRLYYYNKF KDVASTLNKA
    310 320 330 340 350
    KSIIGTTASL QYMKNVFKEK YLLSEDTSGK FSVDKLKFDK LYKMLTEIYT
    360 370 380 390 400
    EDNFVNFFKV INRKTYLNFD KAVFRINIVP DENYTIKDGF NLKGANLSTN
    410 420 430 440 450
    FNGQNTEINS RNFTRLKNFT GLFEFYKLLC VRGIIPFKTK SLDEGYNKAL
    460 470 480 490 500
    NDLCIKVNNW DLFFSPSEDN FTNDLDKVEE ITADTNIEAA EENISLDLIQ
    510 520 530 540 550
    QYYLTFDFDN EPENISIENL SSDIIGQLEP MPNIERFPNG KKYELDKYTM
    560 570 580 590 600
    FHYLRAQEFE HGDSRIILTN SAEEALLKPN VAYTFFSSKY VKKINKAVEA
    610 620 630 640 650
    FMFLNWAEEL VYDFTDETNE VTTMDKIADI TIIVPYIGPA LNIGNMLSKG
    660 670 680 690 700
    EFVEAIIFTG VVAMLEFIPE YALPVFGTFA IVSYIANKVL TVQTINNALS
    710 720 730 740 750
    KRNEKWDEVY KYTVTNWLAK VNTQIDLIRE KMKKALENQA EATKAIINYQ
    760 770 780 790 800
    YNQYTEEEKN NINFNIDDLS SKLNESINSA MININKFLDQ CSVSYLMNSM
    810 820 830 840 850
    IPYAVKRLKD FDASVRDVLL KYIYDNRGTL VLQVDRLKDE VNNTLSADIP
    860 870 880 890 900
    FQLSKYVDNK KLLSTFTEYI KNIVNTSILS IVYKKDDLID LSRYGAKINI
    910 920 930 940 950
    GDRVYYDSID KNQIKLINLE SSTIEVILKN AIVYNSMYEN FSTSFWIKIP
    960 970 980 990 1000
    KYFSKINLNN EYTIINCIEN NSGWKVSLNY GEIIWTLQDN KQNIQRVVFK
    1010 1020 1030 1040 1050
    YSQMVNISDY INRWIFVTIT NNRLTKSKIY INGRLIDQKP ISNLGNIHAS
    1060 1070 1080 1090 1100
    NKIMFKLDGC RDPRRYIMIK YFNLFDKELN EKEIKDLYDS QSNSGILKDF
    1110 1120 1130 1140 1150
    WGNYLQYDKP YYMLNLFDPN KYVDVNNIGI RGYMYLKGPR GSVVTTNIYL
    1160 1170 1180 1190 1200
    NSTLYEGTKF IIKKYASGNE DNIVRNNDRV YINVVVKNKE YRLATNASQA
    1210 1220 1230 1240 1250
    GVEKILSALE IPDVGNLSQV VVMKSKDDQG IRNKCKMNLQ DNNGNDIGFI
    1260 1270 1280 1290
    GFHLYDNIAK LVASNWYNRQ VGKASRTFGC SWEFIPVDDG WGESSL
    Length:1,296
    Mass (Da):149,411
    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:i6F12E7BF28ED69D1
    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
    X73423 Genomic DNA Translation: CAA51824.1
    CP001581 Genomic DNA Translation: ACO83782.1
    X87974 Genomic DNA Translation: CAA61234.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    I40645

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_012703873.1, NC_012563.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ACO83782; ACO83782; CLM_0897

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    cby:CLM_0897

    <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
    X73423 Genomic DNA Translation: CAA51824.1
    CP001581 Genomic DNA Translation: ACO83782.1
    X87974 Genomic DNA Translation: CAA61234.1
    PIRiI40645
    RefSeqiWP_012703873.1, NC_012563.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

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    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
    1E1HX-ray1.80A/C10-250[»]
    B/D251-416[»]
    2G7KX-ray2.80A/B3-426[»]
    2G7NX-ray1.90A3-426[»]
    2G7PX-ray2.30A/B3-426[»]
    2G7QX-ray2.41A/B3-426[»]
    5MOYX-ray2.30A871-1296[»]
    6ES1X-ray2.00A874-1296[»]
    SMRiQ45894
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    DIPiDIP-437N
    STRINGi536232.CLM_0897

    Protein family/group databases

    Allergomei12104 Clo bo Toxin

    Genome annotation databases

    EnsemblBacteriaiACO83782; ACO83782; CLM_0897
    KEGGicby:CLM_0897

    Phylogenomic databases

    HOGENOMiHOG000234384
    KOiK06011
    OMAiDEGYNKA

    Enzyme and pathway databases

    BioCyciCBOT536232:G1GVA-850-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiQ45894

    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

    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 nameiBXA2_CLOBJ
    <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: Q45894
    Secondary accession number(s): C1FUH9, P77780
    <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: January 23, 2002
    Last sequence update: January 23, 2007
    Last modified: December 11, 2019
    This is version 152 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

    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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