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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

Zn2+By similarityNote: 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 – 238Combined sources
Helixi25 – 273Combined sources
Turni28 – 314Combined sources
Beta strandi34 – 407Combined sources
Beta strandi43 – 464Combined sources
Helixi56 – 594Combined sources
Beta strandi63 – 664Combined sources
Beta strandi72 – 743Combined sources
Turni76 – 794Combined sources
Helixi82 – 9918Combined sources
Helixi103 – 11412Combined sources
Beta strandi122 – 1243Combined sources
Turni134 – 1363Combined sources
Beta strandi137 – 1415Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi151 – 1555Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi176 – 1794Combined sources
Helixi182 – 1843Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi191 – 1944Combined sources
Beta strandi197 – 2037Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi219 – 2213Combined sources
Helixi224 – 23916Combined sources
Helixi266 – 2727Combined sources
Helixi276 – 2794Combined sources
Helixi282 – 30524Combined sources
Beta strandi308 – 3114Combined sources
Helixi317 – 32711Combined sources
Beta strandi330 – 3323Combined sources
Beta strandi338 – 3403Combined sources
Helixi342 – 35413Combined sources
Helixi358 – 3658Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi378 – 3847Combined sources
Turni389 – 3913Combined sources
Turni394 – 3963Combined sources
Helixi401 – 4033Combined sources
Helixi407 – 4126Combined sources
Turni414 – 4163Combined sources
Helixi418 – 4203Combined sources
Beta strandi421 – 4233Combined sources
Helixi426 – 4283Combined sources
Beta strandi433 – 4375Combined sources
Beta strandi446 – 4505Combined sources
Helixi451 – 4533Combined sources
Helixi460 – 4623Combined sources
Helixi466 – 4683Combined sources
Beta strandi471 – 4733Combined sources
Helixi488 – 4936Combined sources
Beta strandi495 – 4984Combined sources
Beta strandi506 – 5083Combined sources
Beta strandi524 – 5318Combined sources
Helixi537 – 5426Combined sources
Beta strandi554 – 5574Combined sources
Helixi559 – 5646Combined sources
Beta strandi568 – 5703Combined sources
Helixi575 – 5817Combined sources
Helixi587 – 60620Combined sources
Helixi607 – 6093Combined sources
Beta strandi610 – 6123Combined sources
Helixi613 – 6153Combined sources
Beta strandi617 – 6204Combined sources
Helixi624 – 6285Combined sources
Turni631 – 6355Combined sources
Helixi639 – 6468Combined sources
Helixi647 – 6515Combined sources
Beta strandi666 – 6683Combined sources
Helixi675 – 70733Combined sources
Helixi709 – 73830Combined sources
Helixi743 – 7475Combined sources
Helixi753 – 78634Combined sources
Helixi788 – 81225Combined sources
Helixi814 – 8174Combined sources
Turni819 – 8246Combined sources
Helixi825 – 8317Combined sources
Helixi840 – 8423Combined sources
Helixi847 – 85711Combined sources
Helixi860 – 8634Combined sources
Beta strandi864 – 8707Combined sources
Beta strandi872 – 8776Combined sources
Beta strandi879 – 8813Combined sources
Beta strandi884 – 8874Combined sources
Beta strandi891 – 8933Combined sources
Beta strandi897 – 9015Combined sources
Beta strandi909 – 9124Combined sources
Beta strandi917 – 9193Combined sources
Beta strandi921 – 9233Combined sources
Beta strandi926 – 9338Combined sources
Helixi939 – 9413Combined sources
Helixi942 – 9476Combined sources
Beta strandi949 – 9579Combined sources
Beta strandi960 – 9678Combined sources
Beta strandi970 – 9767Combined sources
Beta strandi978 – 9803Combined sources
Beta strandi982 – 9887Combined sources
Beta strandi991 – 9955Combined sources
Beta strandi1003 – 10097Combined sources
Beta strandi1011 – 10188Combined sources
Beta strandi1021 – 10277Combined sources
Beta strandi1038 – 104710Combined sources
Beta strandi1054 – 106411Combined sources
Helixi1068 – 107912Combined sources
Beta strandi1089 – 10913Combined sources
Beta strandi1093 – 10953Combined sources
Beta strandi1097 – 11026Combined sources
Helixi1103 – 11053Combined sources
Beta strandi1108 – 11125Combined sources
Beta strandi1116 – 11238Combined sources
Beta strandi1145 – 11495Combined sources
Turni1153 – 11553Combined sources
Beta strandi1166 – 11738Combined sources
Beta strandi1176 – 11838Combined sources
Beta strandi1188 – 11925Combined sources
Beta strandi1194 – 11985Combined sources
Beta strandi1202 – 12054Combined sources
Beta strandi1208 – 12114Combined sources
Beta strandi1221 – 123111Combined sources
Beta strandi1234 – 124613Combined sources
Beta strandi1248 – 12503Combined sources
Beta strandi1251 – 126010Combined sources
Helixi1263 – 12664Combined sources
Beta strandi1269 – 12713Combined sources
Beta strandi1280 – 12834Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

P10844-1 [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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 138 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