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P10844

- BXB_CLOBO

UniProt

P10844 - BXB_CLOBO

Protein

Botulinum neurotoxin type B

Gene

botB

Organism
Clostridium botulinum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 '76-Gln-|-Phe-77' bond of synaptobrevin-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 bindingi230 – 2301Zinc; catalyticPROSITE-ProRule annotation
    Active sitei231 – 2311PROSITE-ProRule annotation
    Metal bindingi234 – 2341Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: Reactome
    2. protein binding Source: IntAct
    3. 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_200782. Toxicity of botulinum toxin type B (BoNT/B).

    Protein family/group databases

    MEROPSiM27.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Botulinum neurotoxin type B (EC:3.4.24.69)
    Short name:
    BoNT/B
    Alternative name(s):
    Bontoxilysin-B
    Cleaved into the following 2 chains:
    Gene namesi
    Name:botB
    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

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 441440Botulinum neurotoxin B light chainPRO_0000029215Add
    BLAST
    Chaini442 – 1291850Botulinum neurotoxin B heavy chainPRO_0000029216Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi437 ↔ 446Interchain (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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Syt2P291013EBI-7661991,EBI-458017From a different organism.

    Protein-protein interaction databases

    DIPiDIP-42782N.
    IntActiP10844. 1 interaction.
    MINTiMINT-1795550.

    Structurei

    Secondary structure

    1
    1291
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 238
    Helixi25 – 273
    Turni28 – 314
    Beta strandi34 – 407
    Beta strandi43 – 464
    Helixi56 – 594
    Beta strandi63 – 664
    Beta strandi72 – 743
    Turni76 – 794
    Helixi82 – 9918
    Helixi103 – 11412
    Beta strandi122 – 1243
    Turni134 – 1363
    Beta strandi137 – 1415
    Beta strandi145 – 1484
    Beta strandi151 – 1555
    Beta strandi157 – 1615
    Beta strandi171 – 1733
    Beta strandi176 – 1794
    Helixi182 – 1843
    Beta strandi185 – 1873
    Beta strandi191 – 1944
    Beta strandi197 – 2037
    Beta strandi206 – 2083
    Beta strandi210 – 2123
    Beta strandi214 – 2163
    Beta strandi219 – 2213
    Helixi224 – 23916
    Helixi266 – 2727
    Helixi276 – 2794
    Helixi282 – 30524
    Beta strandi308 – 3114
    Helixi317 – 32711
    Beta strandi330 – 3323
    Beta strandi338 – 3403
    Helixi342 – 35413
    Helixi358 – 3658
    Beta strandi373 – 3753
    Beta strandi378 – 3847
    Turni389 – 3913
    Turni394 – 3963
    Helixi401 – 4033
    Helixi407 – 4126
    Turni414 – 4163
    Helixi418 – 4203
    Beta strandi421 – 4233
    Helixi426 – 4283
    Beta strandi433 – 4375
    Beta strandi446 – 4505
    Helixi451 – 4533
    Helixi460 – 4623
    Helixi466 – 4683
    Beta strandi471 – 4733
    Helixi488 – 4936
    Beta strandi495 – 4984
    Beta strandi506 – 5083
    Beta strandi524 – 5318
    Helixi537 – 5426
    Beta strandi554 – 5574
    Helixi559 – 5646
    Beta strandi568 – 5703
    Helixi575 – 5817
    Helixi587 – 60620
    Helixi607 – 6093
    Beta strandi610 – 6123
    Helixi613 – 6153
    Beta strandi617 – 6204
    Helixi624 – 6285
    Turni631 – 6355
    Helixi639 – 6468
    Helixi647 – 6515
    Beta strandi666 – 6683
    Helixi675 – 70733
    Helixi709 – 73830
    Helixi743 – 7475
    Helixi753 – 78634
    Helixi788 – 81225
    Helixi814 – 8174
    Turni819 – 8246
    Helixi825 – 8317
    Helixi840 – 8423
    Helixi847 – 85711
    Helixi860 – 8634
    Beta strandi864 – 8707
    Beta strandi872 – 8776
    Beta strandi879 – 8813
    Beta strandi884 – 8874
    Beta strandi891 – 8933
    Beta strandi897 – 9015
    Beta strandi909 – 9124
    Beta strandi917 – 9193
    Beta strandi921 – 9233
    Beta strandi926 – 9338
    Helixi939 – 9413
    Helixi942 – 9476
    Beta strandi949 – 9579
    Beta strandi960 – 9678
    Beta strandi970 – 9767
    Beta strandi978 – 9803
    Beta strandi982 – 9887
    Beta strandi991 – 9955
    Beta strandi1003 – 10097
    Beta strandi1011 – 10188
    Beta strandi1021 – 10277
    Beta strandi1038 – 104710
    Beta strandi1054 – 106411
    Helixi1068 – 107912
    Beta strandi1089 – 10913
    Beta strandi1093 – 10953
    Beta strandi1097 – 11026
    Helixi1103 – 11053
    Beta strandi1108 – 11125
    Beta strandi1116 – 11238
    Beta strandi1145 – 11495
    Turni1153 – 11553
    Beta strandi1166 – 11738
    Beta strandi1176 – 11838
    Beta strandi1188 – 11925
    Beta strandi1194 – 11985
    Beta strandi1202 – 12054
    Beta strandi1208 – 12114
    Beta strandi1221 – 123111
    Beta strandi1234 – 124613
    Beta strandi1248 – 12503
    Beta strandi1251 – 126010
    Helixi1263 – 12664
    Beta strandi1269 – 12713
    Beta strandi1280 – 12834

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP10844.
    SMRiP10844. Positions 2-425, 854-1291.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10844.

    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. 1 hit.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10844-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVTINNFNY NDPIDNNNII MMEPPFARGT GRYYKAFKIT DRIWIIPERY     50
    TFGYKPEDFN KSSGIFNRDV CEYYDPDYLN TNDKKNIFLQ TMIKLFNRIK 100
    SKPLGEKLLE MIINGIPYLG DRRVPLEEFN TNIASVTVNK LISNPGEVER 150
    KKGIFANLII FGPGPVLNEN ETIDIGIQNH FASREGFGGI MQMKFCPEYV 200
    SVFNNVQENK GASIFNRRGY FSDPALILMH ELIHVLHGLY GIKVDDLPIV 250
    PNEKKFFMQS TDAIQAEELY TFGGQDPSII TPSTDKSIYD KVLQNFRGIV 300
    DRLNKVLVCI SDPNININIY KNKFKDKYKF VEDSEGKYSI DVESFDKLYK 350
    SLMFGFTETN IAENYKIKTR ASYFSDSLPP VKIKNLLDNE IYTIEEGFNI 400
    SDKDMEKEYR GQNKAINKQA YEEISKEHLA VYKIQMCKSV KAPGICIDVD 450
    NEDLFFIADK NSFSDDLSKN ERIEYNTQSN YIENDFPINE LILDTDLISK 500
    IELPSENTES LTDFNVDVPV YEKQPAIKKI FTDENTIFQY LYSQTFPLDI 550
    RDISLTSSFD DALLFSNKVY SFFSMDYIKT ANKVVEAGLF AGWVKQIVND 600
    FVIEANKSNT MDKIADISLI VPYIGLALNV GNETAKGNFE NAFEIAGASI 650
    LLEFIPELLI PVVGAFLLES YIDNKNKIIK TIDNALTKRN EKWSDMYGLI 700
    VAQWLSTVNT QFYTIKEGMY KALNYQAQAL EEIIKYRYNI YSEKEKSNIN 750
    IDFNDINSKL NEGINQAIDN INNFINGCSV SYLMKKMIPL AVEKLLDFDN 800
    TLKKNLLNYI DENKLYLIGS AEYEKSKVNK YLKTIMPFDL SIYTNDTILI 850
    EMFNKYNSEI LNNIILNLRY KDNNLIDLSG YGAKVEVYDG VELNDKNQFK 900
    LTSSANSKIR VTQNQNIIFN SVFLDFSVSF WIRIPKYKND GIQNYIHNEY 950
    TIINCMKNNS GWKISIRGNR IIWTLIDING KTKSVFFEYN IREDISEYIN 1000
    RWFFVTITNN LNNAKIYING KLESNTDIKD IREVIANGEI IFKLDGDIDR 1050
    TQFIWMKYFS IFNTELSQSN IEERYKIQSY SEYLKDFWGN PLMYNKEYYM 1100
    FNAGNKNSYI KLKKDSPVGE ILTRSKYNQN SKYINYRDLY IGEKFIIRRK 1150
    SNSQSINDDI VRKEDYIYLD FFNLNQEWRV YTYKYFKKEE EKLFLAPISD 1200
    SDEFYNTIQI KEYDEQPTYS CQLLFKKDEE STDEIGLIGI HRFYESGIVF 1250
    EEYKDYFCIS KWYLKEVKRK PYNLKLGCNW QFIPKDEGWT E 1291
    Length:1,291
    Mass (Da):150,803
    Last modified:January 23, 2007 - v3
    Checksum:i921DE5C518140DBD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301T → M AA sequence (PubMed:3139097)Curated
    Sequence conflicti218 – 2181R → G in CAA77991. 1 PublicationCurated
    Sequence conflicti225 – 2251A → S in CAA77991. 1 PublicationCurated
    Sequence conflicti464 – 4641S → R AA sequence (PubMed:3139097)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81186 Genomic DNA. Translation: AAA23211.1.
    Z11934 Genomic DNA. Translation: CAA77991.1.
    X70817 Genomic DNA. Translation: CAA50148.1.
    PIRiA48940.

    Cross-referencesi

    Web resourcesi

    BotDB - A Database Resource for Clostridial Neurotoxins

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81186 Genomic DNA. Translation: AAA23211.1 .
    Z11934 Genomic DNA. Translation: CAA77991.1 .
    X70817 Genomic DNA. Translation: CAA50148.1 .
    PIRi A48940.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EPW X-ray 1.90 A 2-1291 [» ]
    1F31 X-ray 2.60 A 2-1291 [» ]
    1F82 X-ray 2.20 A 2-425 [» ]
    1G9A X-ray 2.10 A 2-1291 [» ]
    1G9B X-ray 2.00 A 2-1291 [» ]
    1G9C X-ray 2.35 A 2-1291 [» ]
    1G9D X-ray 2.20 A 2-1291 [» ]
    1I1E X-ray 2.50 A 2-1291 [» ]
    1S0B X-ray 2.00 A 2-1291 [» ]
    1S0C X-ray 2.20 A 2-1291 [» ]
    1S0D X-ray 2.20 A 2-1291 [» ]
    1S0E X-ray 1.90 A 2-1291 [» ]
    1S0F X-ray 2.30 A 2-1291 [» ]
    1S0G X-ray 2.60 A 2-1291 [» ]
    1Z0H X-ray 2.00 A/B 854-1291 [» ]
    2ETF X-ray 2.29 A/B 1-441 [» ]
    2NM1 X-ray 2.15 A 858-1291 [» ]
    2NP0 X-ray 2.62 A 2-1291 [» ]
    2XHL X-ray 2.80 A 1-437 [» ]
    B 446-858 [» ]
    3ZUQ X-ray 2.70 A 1-437 [» ]
    A 446-858 [» ]
    4KBB X-ray 2.30 A/B 857-1291 [» ]
    ProteinModelPortali P10844.
    SMRi P10844. Positions 2-425, 854-1291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-42782N.
    IntActi P10844. 1 interaction.
    MINTi MINT-1795550.

    Chemistry

    BindingDBi P10844.
    ChEMBLi CHEMBL1075064.
    DrugBanki DB00042. Botulinum Toxin Type B.

    Protein family/group databases

    MEROPSi M27.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    Reactomei REACT_200782. Toxicity of botulinum toxin type B (BoNT/B).

    Miscellaneous databases

    EvolutionaryTracei P10844.

    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. 1 hit.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the Clostridium botulinum structural gene encoding the type B neurotoxin and determination of its entire nucleotide sequence."
      Whelan S.M., Elmore M.J., Bodsworth N.J., Brehm J.K., Atkinson T., Minton N.P.
      Appl. Environ. Microbiol. 58:2345-2354(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Szabo E.A., Pemberton J.M., Desmarchelier P.M.
      Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-246.
      Strain: Type B / NCTC 7273.
    3. "Gene probes for identification of the botulinal neurotoxin gene and specific identification of neurotoxin types B, E, and F."
      Campbell K.D., Collins M.D., East A.K.
      J. Clin. Microbiol. 31:2255-2262(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-994.
      Strain: Type B / NCTC 7273.
    4. "Botulinum neurotoxin type B (strain 657): partial sequence and similarity with tetanus toxin."
      Dasgupta B.R., Datta A.
      Biochimie 70:811-817(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-45 AND 442-467.
      Strain: Type B / B-657.
    5. "Botulinum neurotoxins are zinc proteins."
      Schiavo G., Rossetto O., Santucci A., Dasgupta B.R., Montecucco C.
      J. Biol. Chem. 267:23479-23483(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A ZINC-PROTEASE.
    6. "Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin."
      Schiavo G., Benfenati F., Poulain B., Rossetto O., de Laureto P.P., Dasgupta B.R., Montecucco C.
      Nature 359:832-835(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF SUBSTRATE.

    Entry informationi

    Entry nameiBXB_CLOBO
    AccessioniPrimary (citable) accession number: P10844
    Secondary accession number(s): P10843
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 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.

    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