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Entry version 12 (11 Dec 2019)
Sequence version 1 (25 Oct 2017)
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Protein

Botulinum-like toxin eBoNT/J

Gene

A5816_002916

Organism
Enterococcus sp. (strain 3G1_DIV0629)
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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

Strongly resembles a botulinum-type toxin, with the appropriate domains and residues to have proteolytic function, although its C-terminus (which binds to a eukaryotic host cell) is different enough from clostrial botulinum toxins that it might bind another cell target (PubMed:29323697). Might be a precursor of a toxin that binds to an unknown eukaryotic cell receptor(s), and be taken up into the host cell via the endocytic pathway. When the pH of the putative toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the heavy chain forms pores that allows the light chain to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and light chain cleaves its target protein (By similarity).By similarity1 Publication

Miscellaneous

There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C, D, E, F, and G; this protein has not been tested seriologically. New subtypes are quite frequent.Curated
This strain was isolated from cow feces in South Carolina, USA, but whether the cattle were infected with botulism is not known. This locus includes a number of other genes usually associated with the botulinum neurotoxin cluster in Clostridia (botR, hemagglutinin genes and p47 proteins), which might permit the toxin to survive in a host.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.By similarity 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+By similarityNote: Binds 1 zinc ion per subunit (By similarity).By similarity

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 bindingi225Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationBy similarity1 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 sitei226PROSITE-ProRule annotationBy similarity1
Metal bindingi229Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotationBy similarity1 Publication1
Metal bindingi269Zinc; catalyticBy similarity1 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
LigandMetal-binding, Zinc

<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-like toxin eBoNT/J1 Publication
Short name:
eBoNT/J1 Publication
Cleaved into the following 2 chains:
Botulinum-like toxin eBoNT/J light chain (EC:3.4.24.69Curated)
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
ORF Names:A5816_002916
<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>OrganismiEnterococcus sp. (strain 3G1_DIV0629)
<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 identifieri1834176 [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 lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
<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
  • UP000194867 <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: Unassembled WGS sequence

<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

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, Secreted

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004449151 – 1279Botulinum-like toxin eBoNT/JAdd BLAST1279
ChainiPRO_00004449161 – 434Botulinum-like toxin eBoNT/J light chainAdd BLAST434
ChainiPRO_0000444917435 – 1279Botulinum-like toxin eBoNT/J heavy chainAdd BLAST845

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 bondi424 ↔ 438Interchain (between light and heavy chains)By similarity1 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

Might be a disulfide-linked heterodimer of a light chain (LC) and heavy chain (HC).

By similarity

<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>Regioni435 – 843Translocation domain (TD)1 PublicationAdd BLAST409
Regioni476 – 525Belt; not required for channel formationBy similarityAdd BLAST50
Regioni860 – 1080N-terminus of receptor binding domain (N-RBD)By similarityAdd BLAST221
Regioni1081 – 1279C-terminus of receptor binding domain (C-RBD)By similarityAdd BLAST199

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>Motifi1250 – 1253Host ganglioside-binding motifBy similarity1 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

The light chain (LC) has protease activity. HC 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). The N-terminus of the TD wraps an extended belt around the perimeter of the light chain, 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.

<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

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
IPR012928 Toxin_rcpt-bd_N
IPR012500 Toxin_trans

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01742 Peptidase_M27, 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.

A0A242DI27-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVTINDLHYS DPIDEDNIIN MRIPLYDLEV DDQFINHNVP DLKAFQVFPN
60 70 80 90 100
VWVVPERYTF YSTMKNLDAP ANPSRSSYYD PTYLQSDAEK EVFLQQMILL
110 120 130 140 150
FKRINSTQEG QQFLNLLSRS IPVPYESNGD VAMGTTQVIK QMDDKGNVLK
160 170 180 190 200
HRRAHIIIYG PGPDLMAKGS KALTKSRETG RGCMAEIYFS PMYHKTYSTK
210 220 230 240 250
LTNKNSLVDK SVQEFVPDPA VTLIHELCHG LHALYGIDLG NVGSWEFNSN
260 270 280 290 300
PNSLFSSWFS SKEAVNFEEV MTFGGEDVKV IKSEIDKKIP GILNLIKTTV
310 320 330 340 350
EPIINKITDP HDEMLQCLQS KYPSLKGTLG QFFFDDTQLE KDIRDLWMVM
360 370 380 390 400
NETMFAENLK ALTRARYLVP KVENIVQVDI LSPNVYTIDK GFNHLSKGFK
410 420 430 440 450
GQSVSQSYFR KISALARGAV VRACPNPHFS SQRGLSSCIE ILEDDLFIMS
460 470 480 490 500
SKDSFTDTDF SEPSVGPVSY KAKKGADTIL DSTLSNYDFS KEINFTSTVP
510 520 530 540 550
IITVEDPLET DEDVPVISED RTVYVDDYTT FHFLEAQKIG KEVVPTQTKV
560 570 580 590 600
VFTTNMEEAL FDSKKVYTVF ENTASRINEA GTGIANGMMF YQWLKGIVQD
610 620 630 640 650
FTEEATQKDT FDKISDVTMI VPYLGNILNI GNDIRKGDFM GAVELGGVTI
660 670 680 690 700
LLEAIPELTL PVLIGLTIIE DELEKEQVSQ TVYNVLDKRD EKWEEVYGFV
710 720 730 740 750
KQQWWWMVHT QFETRILHAY QALNHQVEAI KANMTYQLAN YRGNQEDKEL
760 770 780 790 800
LEKAIDDTLQ SLYYAVDQAM HNIKRFLIQS SKSYLLNQML PKTKEQLLAF
810 820 830 840 850
DQQTLRNVND FINKNQGVLG ESLAKDLKKK VEKRLTSLPV FNLEDLPISE
860 870 880 890 900
FEDLIHSHEI DIQDSEVLNI GVNNGKIQDL SGENTPLTLG ENLHIVNGRD
910 920 930 940 950
NQAVRLNNQL DSKLEIQSRP NIHFTAFEDF SISIWIRCSM LRNNRNRGQK
960 970 980 990 1000
YTIIQQFNKY GWQLAIQDSV FVWTLHDTFN NQIQLTSGSA LTNKNYLLQN
1010 1020 1030 1040 1050
FWLHITVTNK RSEKSRLYIN GVLQDQKDIS VLGNCHPKEP ILFSIQDNSD
1060 1070 1080 1090 1100
PNYFVRFEQF NVYRKALTDS EVNRLYWKYF EGSYLRDVWG ERLTYNRDYY
1110 1120 1130 1140 1150
MQLSTLPGRG IKREYRTWSG FDYIILSELG TQKIPTHEVT YPKLYQGQKI
1160 1170 1180 1190 1200
TIHSDGKNLE PHVKSNKNIR LKIDDFYIGV VNPFKLPEWR PESGAYVVTT
1210 1220 1230 1240 1250
YNHAEDLCLY FRTRSSSQSL YYGQLIMNDG RNKSLLNYTL KGSTYWIWSS
1260 1270
AWYYENYNTS SKTAGNWYFI PVDEGWKED
Length:1,279
Mass (Da):147,267
Last modified:October 25, 2017 - 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:i9619E3D0C227D82C
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
NGLI01000004 Genomic DNA Translation: OTO22244.1

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
NGLI01000004 Genomic DNA Translation: OTO22244.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

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
IPR012928 Toxin_rcpt-bd_N
IPR012500 Toxin_trans
PfamiView protein in Pfam
PF01742 Peptidase_M27, 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 nameiBXJ_ENTS3
<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: A0A242DI27
<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 18, 2018
Last sequence update: October 25, 2017
Last modified: December 11, 2019
This is version 12 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
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