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P10844 (BXB_CLOBO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Botulinum neurotoxin type B

Short name=BoNT/B
EC=3.4.24.69
Alternative name(s):
Bontoxilysin-B
Gene names
Name:botB
OrganismClostridium botulinum
Taxonomic identifier1491 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length1291 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

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.

Subcellular location

Botulinum neurotoxin B light chain: Secreted. Host cytoplasmhost cytosol.

Botulinum neurotoxin B heavy chain: Secreted. Host cell junctionhost synapsehost presynaptic cell membrane Potential.

Miscellaneous

There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.

Sequence similarities

Belongs to the peptidase M27 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Syt2P291013EBI-7661991,EBI-458017From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 441440Botulinum neurotoxin B light chain
PRO_0000029215
Chain442 – 1291850Botulinum neurotoxin B heavy chain
PRO_0000029216

Sites

Active site2311 By similarity
Metal binding2301Zinc; catalytic By similarity
Metal binding2341Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond437 ↔ 446Interchain (between light and heavy chains) Probable

Experimental info

Sequence conflict301T → M AA sequence Ref.4
Sequence conflict2181R → G in CAA77991. Ref.2
Sequence conflict2251A → S in CAA77991. Ref.2
Sequence conflict4641S → R AA sequence Ref.4

Secondary structure

................................................................................................................................................................................................................................................... 1291
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10844 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 921DE5C518140DBD

FASTA1,291150,803
        10         20         30         40         50         60 
MPVTINNFNY NDPIDNNNII MMEPPFARGT GRYYKAFKIT DRIWIIPERY TFGYKPEDFN 

        70         80         90        100        110        120 
KSSGIFNRDV CEYYDPDYLN TNDKKNIFLQ TMIKLFNRIK SKPLGEKLLE MIINGIPYLG 

       130        140        150        160        170        180 
DRRVPLEEFN TNIASVTVNK LISNPGEVER KKGIFANLII FGPGPVLNEN ETIDIGIQNH 

       190        200        210        220        230        240 
FASREGFGGI MQMKFCPEYV SVFNNVQENK GASIFNRRGY FSDPALILMH ELIHVLHGLY 

       250        260        270        280        290        300 
GIKVDDLPIV PNEKKFFMQS TDAIQAEELY TFGGQDPSII TPSTDKSIYD KVLQNFRGIV 

       310        320        330        340        350        360 
DRLNKVLVCI SDPNININIY KNKFKDKYKF VEDSEGKYSI DVESFDKLYK SLMFGFTETN 

       370        380        390        400        410        420 
IAENYKIKTR ASYFSDSLPP VKIKNLLDNE IYTIEEGFNI SDKDMEKEYR GQNKAINKQA 

       430        440        450        460        470        480 
YEEISKEHLA VYKIQMCKSV KAPGICIDVD NEDLFFIADK NSFSDDLSKN ERIEYNTQSN 

       490        500        510        520        530        540 
YIENDFPINE LILDTDLISK IELPSENTES LTDFNVDVPV YEKQPAIKKI FTDENTIFQY 

       550        560        570        580        590        600 
LYSQTFPLDI RDISLTSSFD DALLFSNKVY SFFSMDYIKT ANKVVEAGLF AGWVKQIVND 

       610        620        630        640        650        660 
FVIEANKSNT MDKIADISLI VPYIGLALNV GNETAKGNFE NAFEIAGASI LLEFIPELLI 

       670        680        690        700        710        720 
PVVGAFLLES YIDNKNKIIK TIDNALTKRN EKWSDMYGLI VAQWLSTVNT QFYTIKEGMY 

       730        740        750        760        770        780 
KALNYQAQAL EEIIKYRYNI YSEKEKSNIN IDFNDINSKL NEGINQAIDN INNFINGCSV 

       790        800        810        820        830        840 
SYLMKKMIPL AVEKLLDFDN TLKKNLLNYI DENKLYLIGS AEYEKSKVNK YLKTIMPFDL 

       850        860        870        880        890        900 
SIYTNDTILI EMFNKYNSEI LNNIILNLRY KDNNLIDLSG YGAKVEVYDG VELNDKNQFK 

       910        920        930        940        950        960 
LTSSANSKIR VTQNQNIIFN SVFLDFSVSF WIRIPKYKND GIQNYIHNEY TIINCMKNNS 

       970        980        990       1000       1010       1020 
GWKISIRGNR IIWTLIDING KTKSVFFEYN IREDISEYIN RWFFVTITNN LNNAKIYING 

      1030       1040       1050       1060       1070       1080 
KLESNTDIKD IREVIANGEI IFKLDGDIDR TQFIWMKYFS IFNTELSQSN IEERYKIQSY 

      1090       1100       1110       1120       1130       1140 
SEYLKDFWGN PLMYNKEYYM FNAGNKNSYI KLKKDSPVGE ILTRSKYNQN SKYINYRDLY 

      1150       1160       1170       1180       1190       1200 
IGEKFIIRRK SNSQSINDDI VRKEDYIYLD FFNLNQEWRV YTYKYFKKEE EKLFLAPISD 

      1210       1220       1230       1240       1250       1260 
SDEFYNTIQI KEYDEQPTYS CQLLFKKDEE STDEIGLIGI HRFYESGIVF EEYKDYFCIS 

      1270       1280       1290 
KWYLKEVKRK PYNLKLGCNW QFIPKDEGWT E 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81186 Genomic DNA. Translation: AAA23211.1.
Z11934 Genomic DNA. Translation: CAA77991.1.
X70817 Genomic DNA. Translation: CAA50148.1.
PIRA48940.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EPWX-ray1.90A2-1290[»]
1F31X-ray2.60A2-1290[»]
1F82X-ray2.20A2-424[»]
1G9AX-ray2.10A2-1290[»]
1G9BX-ray2.00A2-1290[»]
1G9CX-ray2.35A2-1290[»]
1G9DX-ray2.20A2-1290[»]
1I1EX-ray2.50A2-1290[»]
1S0BX-ray2.00A2-1290[»]
1S0CX-ray2.20A2-1290[»]
1S0DX-ray2.20A2-1290[»]
1S0EX-ray1.90A2-1290[»]
1S0FX-ray2.30A2-1290[»]
1S0GX-ray2.60A2-1290[»]
1Z0HX-ray2.00A/B854-1290[»]
2ETFX-ray2.29A/B1-441[»]
2NM1X-ray2.15A858-1290[»]
2NP0X-ray2.62A2-1290[»]
2XHLX-ray2.80A1-437[»]
B446-858[»]
3ZUQX-ray2.70A1-858[»]
4KBBX-ray2.30A/B857-1291[»]
ProteinModelPortalP10844.
SMRP10844. Positions 2-425, 854-1291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-42782N.
IntActP10844. 1 interaction.
MINTMINT-1795550.

Chemistry

BindingDBP10844.
ChEMBLCHEMBL1075064.
DrugBankDB00042. Botulinum Toxin Type B.

Protein family/group databases

MEROPSM27.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_13685. Neuronal System.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProIPR008985. 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]
PfamPF01742. 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]
PRINTSPR00760. BONTOXILYSIN.
SUPFAMSSF49899. SSF49899. 1 hit.
SSF50386. SSF50386. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10844.

Entry information

Entry nameBXB_CLOBO
AccessionPrimary (citable) accession number: P10844
Secondary accession number(s): P10843
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references