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P10844

- BXB_CLOBO

UniProt

P10844 - BXB_CLOBO

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Protein

Botulinum neurotoxin type B

Gene

botB

Organism
Clostridium botulinum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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 cytoplasm Source: UniProtKB-KW
  2. host cell junction Source: UniProtKB-KW
  3. host cell synapse Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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
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.
InterProiIPR013320. ConA-like_dom.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPVTINNFNY NDPIDNNNII MMEPPFARGT GRYYKAFKIT DRIWIIPERY
60 70 80 90 100
TFGYKPEDFN KSSGIFNRDV CEYYDPDYLN TNDKKNIFLQ TMIKLFNRIK
110 120 130 140 150
SKPLGEKLLE MIINGIPYLG DRRVPLEEFN TNIASVTVNK LISNPGEVER
160 170 180 190 200
KKGIFANLII FGPGPVLNEN ETIDIGIQNH FASREGFGGI MQMKFCPEYV
210 220 230 240 250
SVFNNVQENK GASIFNRRGY FSDPALILMH ELIHVLHGLY GIKVDDLPIV
260 270 280 290 300
PNEKKFFMQS TDAIQAEELY TFGGQDPSII TPSTDKSIYD KVLQNFRGIV
310 320 330 340 350
DRLNKVLVCI SDPNININIY KNKFKDKYKF VEDSEGKYSI DVESFDKLYK
360 370 380 390 400
SLMFGFTETN IAENYKIKTR ASYFSDSLPP VKIKNLLDNE IYTIEEGFNI
410 420 430 440 450
SDKDMEKEYR GQNKAINKQA YEEISKEHLA VYKIQMCKSV KAPGICIDVD
460 470 480 490 500
NEDLFFIADK NSFSDDLSKN ERIEYNTQSN YIENDFPINE LILDTDLISK
510 520 530 540 550
IELPSENTES LTDFNVDVPV YEKQPAIKKI FTDENTIFQY LYSQTFPLDI
560 570 580 590 600
RDISLTSSFD DALLFSNKVY SFFSMDYIKT ANKVVEAGLF AGWVKQIVND
610 620 630 640 650
FVIEANKSNT MDKIADISLI VPYIGLALNV GNETAKGNFE NAFEIAGASI
660 670 680 690 700
LLEFIPELLI PVVGAFLLES YIDNKNKIIK TIDNALTKRN EKWSDMYGLI
710 720 730 740 750
VAQWLSTVNT QFYTIKEGMY KALNYQAQAL EEIIKYRYNI YSEKEKSNIN
760 770 780 790 800
IDFNDINSKL NEGINQAIDN INNFINGCSV SYLMKKMIPL AVEKLLDFDN
810 820 830 840 850
TLKKNLLNYI DENKLYLIGS AEYEKSKVNK YLKTIMPFDL SIYTNDTILI
860 870 880 890 900
EMFNKYNSEI LNNIILNLRY KDNNLIDLSG YGAKVEVYDG VELNDKNQFK
910 920 930 940 950
LTSSANSKIR VTQNQNIIFN SVFLDFSVSF WIRIPKYKND GIQNYIHNEY
960 970 980 990 1000
TIINCMKNNS GWKISIRGNR IIWTLIDING KTKSVFFEYN IREDISEYIN
1010 1020 1030 1040 1050
RWFFVTITNN LNNAKIYING KLESNTDIKD IREVIANGEI IFKLDGDIDR
1060 1070 1080 1090 1100
TQFIWMKYFS IFNTELSQSN IEERYKIQSY SEYLKDFWGN PLMYNKEYYM
1110 1120 1130 1140 1150
FNAGNKNSYI KLKKDSPVGE ILTRSKYNQN SKYINYRDLY IGEKFIIRRK
1160 1170 1180 1190 1200
SNSQSINDDI VRKEDYIYLD FFNLNQEWRV YTYKYFKKEE EKLFLAPISD
1210 1220 1230 1240 1250
SDEFYNTIQI KEYDEQPTYS CQLLFKKDEE STDEIGLIGI HRFYESGIVF
1260 1270 1280 1290
EEYKDYFCIS KWYLKEVKRK PYNLKLGCNW QFIPKDEGWT E
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.

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 IPR013320. ConA-like_dom.
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 29, 2014
This is version 137 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