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P19321

- BXD_CLOBO

UniProt

P19321 - BXD_CLOBO

Protein

Botulinum neurotoxin type D

Gene

botD

Organism
Clostridium botulinum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Botulinum toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves the '60-Lys-|-Leu-61' bond of synaptobrevins-1 and -2.

    Catalytic activityi

    Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi229 – 2291Zinc; catalytic
    Active sitei230 – 2301PROSITE-ProRule annotation
    Metal bindingi233 – 2331Zinc; catalytic
    Metal bindingi269 – 2691Zinc; catalytic

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: Reactome
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. inhibition of neurotransmitter uptake Source: InterPro
    2. neurotransmitter secretion Source: Reactome
    3. pathogenesis Source: UniProtKB-KW
    4. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200617. Toxicity of botulinum toxin type D (BoNT/D).

    Protein family/group databases

    MEROPSiM27.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Botulinum neurotoxin type D (EC:3.4.24.69)
    Short name:
    BoNT/D
    Alternative name(s):
    Bontoxilysin-D
    Cleaved into the following 2 chains:
    Gene namesi
    Name:botD
    OrganismiClostridium botulinum
    Taxonomic identifieri1491 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    Subcellular locationi

    GO - Cellular componenti

    1. host cell cytosol Source: UniProtKB-SubCell
    2. host cell junction Source: UniProtKB-KW
    3. host cell presynaptic membrane Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host cell junction, Host cell membrane, Host cytoplasm, Host membrane, Host synapse, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 442442Botulinum neurotoxin D light chainPRO_0000029219Add
    BLAST
    Chaini443 – 1276834Botulinum neurotoxin D heavy chainPRO_0000029220Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi437 ↔ 450Interchain (between light and heavy chains)Curated

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Disulfide-linked heterodimer of a light chain (L) and a heavy chain (H). The light chain has the pharmacological activity, while the N- and C-terminal of the heavy chain mediate channel formation and toxin binding, respectively.1 Publication

    Structurei

    Secondary structure

    1
    1276
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 238
    Beta strandi34 – 407
    Beta strandi43 – 464
    Turni67 – 693
    Turni74 – 774
    Helixi80 – 9718
    Helixi101 – 11212
    Beta strandi126 – 1283
    Turni132 – 1343
    Beta strandi136 – 1427
    Beta strandi145 – 1528
    Beta strandi155 – 1595
    Helixi181 – 1833
    Beta strandi184 – 1863
    Beta strandi190 – 1934
    Beta strandi201 – 2033
    Beta strandi218 – 2203
    Helixi223 – 23816
    Helixi267 – 2737
    Helixi275 – 2806
    Helixi283 – 30624
    Beta strandi309 – 3124
    Helixi313 – 3186
    Helixi319 – 32911
    Helixi344 – 35512
    Helixi360 – 3667
    Turni390 – 3923
    Turni395 – 3973
    Helixi403 – 4053
    Helixi411 – 4133
    Turni415 – 4173
    Beta strandi421 – 4233
    Helixi864 – 8674
    Beta strandi868 – 8758
    Beta strandi878 – 8814
    Beta strandi883 – 8853
    Beta strandi888 – 8914
    Beta strandi896 – 9016
    Beta strandi904 – 9074
    Beta strandi909 – 9113
    Beta strandi914 – 9174
    Beta strandi931 – 9399
    Helixi941 – 9444
    Beta strandi948 – 9547
    Beta strandi957 – 9593
    Beta strandi961 – 9677
    Beta strandi970 – 9767
    Beta strandi982 – 9887
    Turni991 – 9933
    Beta strandi1003 – 10097
    Beta strandi1013 – 10197
    Beta strandi1022 – 10287
    Beta strandi1040 – 10445
    Beta strandi1055 – 106511
    Helixi1069 – 107911
    Turni1080 – 10834
    Beta strandi1090 – 10923
    Beta strandi1098 – 11036
    Beta strandi1109 – 11146
    Beta strandi1117 – 11226
    Beta strandi1135 – 11395
    Beta strandi1150 – 11523
    Beta strandi1154 – 11618
    Beta strandi1164 – 11707
    Beta strandi1188 – 11969
    Helixi1201 – 12033
    Beta strandi1204 – 12096
    Beta strandi1218 – 12225
    Beta strandi1224 – 12263
    Beta strandi1228 – 12358
    Beta strandi1245 – 12539
    Helixi1255 – 12573
    Helixi1261 – 12633
    Beta strandi1265 – 12684

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FPQX-ray1.65A1-436[»]
    3N7JX-ray2.00A862-1276[»]
    3OBRX-ray1.72A863-1276[»]
    3OBTX-ray2.00A863-1276[»]
    3OGGX-ray1.65A863-1276[»]
    3RMXX-ray2.75A/B/C/D862-1276[»]
    3RMYX-ray2.30A/B/C/D862-1276[»]
    ProteinModelPortaliP19321.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19321.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M27 family.Curated

    Keywords - Domaini

    Transmembrane

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    3.90.1240.10. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR011065. Kunitz_inhibitor_ST1-like.
    IPR000395. Neurotox_Zn_protease.
    IPR013104. Toxin_rcpt-bd_C.
    IPR012928. Toxin_rcpt-bd_N.
    IPR012500. Toxin_trans.
    [Graphical view]
    PfamiPF01742. Peptidase_M27. 1 hit.
    PF07951. Toxin_R_bind_C. 1 hit.
    PF07953. Toxin_R_bind_N. 1 hit.
    PF07952. Toxin_trans. 1 hit.
    [Graphical view]
    PRINTSiPR00760. BONTOXILYSIN.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF50386. SSF50386. 2 hits.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P19321-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTWPVKDFNY SDPVNDNDIL YLRIPQNKLI TTPVKAFMIT QNIWVIPERF     50
    SSDTNPSLSK PPRPTSKYQS YYDPSYLSTD EQKDTFLKGI IKLFKRINER 100
    DIGKKLINYL VVGSPFMGDS STPEDTFDFT RHTTNIAVEK FENGSWKVTN 150
    IITPSVLIFG PLPNILDYTA SLTLQGQQSN PSFEGFGTLS ILKVAPEFLL 200
    TFSDVTSNQS SAVLGKSIFC MDPVIALMHE LTHSLHQLYG INIPSDKRIR 250
    PQVSEGFFSQ DGPNVQFEEL YTFGGLDVEI IPQIERSQLR EKALGHYKDI 300
    AKRLNNINKT IPSSWISNID KYKKIFSEKY NFDKDNTGNF VVNIDKFNSL 350
    YSDLTNVMSE VVYSSQYNVK NRTHYFSRHY LPVFANILDD NIYTIRDGFN 400
    LTNKGFNIEN SGQNIERNPA LQKLSSESVV DLFTKVCLRL TKNSRDDSTC 450
    IKVKNNRLPY VADKDSISQE IFENKIITDE TNVQNYSDKF SLDESILDGQ 500
    VPINPEIVDP LLPNVNMEPL NLPGEEIVFY DDITKYVDYL NSYYYLESQK 550
    LSNNVENITL TTSVEEALGY SNKIYTFLPS LAEKVNKGVQ AGLFLNWANE 600
    VVEDFTTNIM KKDTLDKISD VSVIIPYIGP ALNIGNSALR GNFNQAFATA 650
    GVAFLLEGFP EFTIPALGVF TFYSSIQERE KIIKTIENCL EQRVKRWKDS 700
    YQWMVSNWLS RITTQFNHIN YQMYDSLSYQ ADAIKAKIDL EYKKYSGSDK 750
    ENIKSQVENL KNSLDVKISE AMNNINKFIR ECSVTYLFKN MLPKVIDELN 800
    KFDLRTKTEL INLIDSHNII LVGEVDRLKA KVNESFENTM PFNIFSYTNN 850
    SLLKDIINEY FNSINDSKIL SLQNKKNALV DTSGYNAEVR VGDNVQLNTI 900
    YTNDFKLSSS GDKIIVNLNN NILYSAIYEN SSVSFWIKIS KDLTNSHNEY 950
    TIINSIEQNS GWKLCIRNGN IEWILQDVNR KYKSLIFDYS ESLSHTGYTN 1000
    KWFFVTITNN IMGYMKLYIN GELKQSQKIE DLDEVKLDKT IVFGIDENID 1050
    ENQMLWIRDF NIFSKELSNE DINIVYEGQI LRNVIKDYWG NPLKFDTEYY 1100
    IINDNYIDRY IAPESNVLVL VQYPDRSKLY TGNPITIKSV SDKNPYSRIL 1150
    NGDNIILHML YNSRKYMIIR DTDTIYATQG GECSQNCVYA LKLQSNLGNY 1200
    GIGIFSIKNI VSKNKYCSQI FSSFRENTML LADIYKPWRF SFKNAYTPVA 1250
    VTNYETKLLS TSSFWKFISR DPGWVE 1276
    Length:1,276
    Mass (Da):146,872
    Last modified:November 1, 1990 - v1
    Checksum:iC1EC50F46C8233E2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 162ND → PV in strain: D-SA.
    Natural varianti17 – 182ND → LQ in strain: D-1873.
    Natural varianti452 – 4521K → Q in strain: D-SA.
    Natural varianti457 – 4571R → F in strain: D-1873.
    Natural varianti457 – 4571R → T in strain: D-SA.
    Natural varianti462 – 4621A → D in strain: D-1873.
    Natural varianti489 – 4891K → N in strain: CB16.
    Natural varianti644 – 6441N → K in strain: CB16.
    Natural varianti1122 – 11221Q → R in strain: CB16.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54254 Genomic DNA. Translation: CAA38175.1.
    S49407 Genomic DNA. Translation: AAB24244.1.
    PIRiS11455.

    Cross-referencesi

    Web resourcesi

    BotDB - A Database Resource for Clostridial Neurotoxins

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54254 Genomic DNA. Translation: CAA38175.1 .
    S49407 Genomic DNA. Translation: AAB24244.1 .
    PIRi S11455.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FPQ X-ray 1.65 A 1-436 [» ]
    3N7J X-ray 2.00 A 862-1276 [» ]
    3OBR X-ray 1.72 A 863-1276 [» ]
    3OBT X-ray 2.00 A 863-1276 [» ]
    3OGG X-ray 1.65 A 863-1276 [» ]
    3RMX X-ray 2.75 A/B/C/D 862-1276 [» ]
    3RMY X-ray 2.30 A/B/C/D 862-1276 [» ]
    ProteinModelPortali P19321.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M27.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    Reactomei REACT_200617. Toxicity of botulinum toxin type D (BoNT/D).

    Miscellaneous databases

    EvolutionaryTracei P19321.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    3.90.1240.10. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR011065. Kunitz_inhibitor_ST1-like.
    IPR000395. Neurotox_Zn_protease.
    IPR013104. Toxin_rcpt-bd_C.
    IPR012928. Toxin_rcpt-bd_N.
    IPR012500. Toxin_trans.
    [Graphical view ]
    Pfami PF01742. Peptidase_M27. 1 hit.
    PF07951. Toxin_R_bind_C. 1 hit.
    PF07953. Toxin_R_bind_N. 1 hit.
    PF07952. Toxin_trans. 1 hit.
    [Graphical view ]
    PRINTSi PR00760. BONTOXILYSIN.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF50386. SSF50386. 2 hits.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Type D / BVD/-3.
    2. "The complete amino acid sequence of the Clostridium botulinum type D neurotoxin, deduced by nucleotide sequence analysis of the encoding phage d-16 phi genome."
      Sunagawa H., Ohyama T., Watanabe T., Inoue K.
      J. Vet. Med. Sci. 54:905-913(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Type D / CB-16.
    3. "Molecular diversity of neurotoxins from Clostridium botulinum type D strains."
      Moriishi K., Syuto B., Kubo S., Oguma K.
      Infect. Immun. 57:2886-2891(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Strain: Type D / D-1873 and Type D / South African.
    4. "Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin."
      Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F., Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H.
      J. Biol. Chem. 269:12764-12772(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF SUBSTRATE.
    5. "Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity."
      Arndt J.W., Chai Q., Christian T., Stevens R.C.
      Biochemistry 45:3255-3262(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-436 IN COMPLEX WITH ZINC IONS.

    Entry informationi

    Entry nameiBXD_CLOBO
    AccessioniPrimary (citable) accession number: P19321
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
    Botulinum type D neurotoxin is synthesized by D strains of C.botulinum which carry the appropriate bacteriophage.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

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

    External Data

    Dasty 3