Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Botulinum neurotoxin type B

Gene

botB

Organism
Clostridium botulinum
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi230Zinc; catalyticPROSITE-ProRule annotation1
Active sitei231PROSITE-ProRule annotation1
Metal bindingi234Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250958. 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

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075064.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000292152 – 441Botulinum neurotoxin B light chainAdd BLAST440
ChainiPRO_0000029216442 – 1291Botulinum neurotoxin B heavy chainAdd BLAST850

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactor.
MINTiMINT-1795550.
STRINGi445335.CBN_0875.

Chemistry databases

BindingDBiP10844.

Structurei

Secondary structure

11291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 23Combined sources8
Helixi25 – 27Combined sources3
Turni28 – 31Combined sources4
Beta strandi34 – 40Combined sources7
Beta strandi43 – 46Combined sources4
Helixi56 – 59Combined sources4
Beta strandi63 – 66Combined sources4
Beta strandi72 – 74Combined sources3
Turni76 – 79Combined sources4
Helixi82 – 99Combined sources18
Helixi103 – 114Combined sources12
Beta strandi122 – 124Combined sources3
Turni134 – 136Combined sources3
Beta strandi137 – 141Combined sources5
Beta strandi145 – 148Combined sources4
Beta strandi151 – 155Combined sources5
Beta strandi157 – 161Combined sources5
Beta strandi171 – 173Combined sources3
Beta strandi176 – 179Combined sources4
Helixi182 – 184Combined sources3
Beta strandi185 – 187Combined sources3
Beta strandi191 – 194Combined sources4
Beta strandi197 – 203Combined sources7
Beta strandi206 – 208Combined sources3
Beta strandi210 – 212Combined sources3
Beta strandi214 – 216Combined sources3
Beta strandi219 – 221Combined sources3
Helixi224 – 239Combined sources16
Helixi266 – 272Combined sources7
Helixi276 – 279Combined sources4
Helixi282 – 305Combined sources24
Beta strandi308 – 311Combined sources4
Helixi317 – 327Combined sources11
Beta strandi330 – 332Combined sources3
Beta strandi338 – 340Combined sources3
Helixi342 – 354Combined sources13
Helixi358 – 365Combined sources8
Beta strandi373 – 375Combined sources3
Beta strandi378 – 384Combined sources7
Turni389 – 391Combined sources3
Turni394 – 396Combined sources3
Helixi401 – 403Combined sources3
Helixi407 – 412Combined sources6
Turni414 – 416Combined sources3
Helixi418 – 420Combined sources3
Beta strandi421 – 423Combined sources3
Helixi426 – 428Combined sources3
Beta strandi433 – 437Combined sources5
Beta strandi446 – 450Combined sources5
Helixi451 – 453Combined sources3
Helixi460 – 462Combined sources3
Helixi466 – 468Combined sources3
Beta strandi471 – 473Combined sources3
Helixi488 – 493Combined sources6
Beta strandi495 – 498Combined sources4
Beta strandi506 – 508Combined sources3
Beta strandi524 – 531Combined sources8
Helixi537 – 542Combined sources6
Beta strandi554 – 557Combined sources4
Helixi559 – 564Combined sources6
Beta strandi568 – 570Combined sources3
Helixi575 – 581Combined sources7
Helixi587 – 606Combined sources20
Helixi607 – 609Combined sources3
Beta strandi610 – 612Combined sources3
Helixi613 – 615Combined sources3
Beta strandi617 – 620Combined sources4
Helixi624 – 628Combined sources5
Turni631 – 635Combined sources5
Helixi639 – 646Combined sources8
Helixi647 – 651Combined sources5
Beta strandi666 – 668Combined sources3
Helixi675 – 707Combined sources33
Helixi709 – 738Combined sources30
Helixi743 – 747Combined sources5
Helixi753 – 786Combined sources34
Helixi788 – 812Combined sources25
Helixi814 – 817Combined sources4
Turni819 – 824Combined sources6
Helixi825 – 831Combined sources7
Helixi840 – 842Combined sources3
Helixi847 – 857Combined sources11
Helixi860 – 863Combined sources4
Beta strandi864 – 870Combined sources7
Beta strandi872 – 877Combined sources6
Beta strandi879 – 881Combined sources3
Beta strandi884 – 887Combined sources4
Beta strandi891 – 893Combined sources3
Beta strandi897 – 901Combined sources5
Beta strandi909 – 912Combined sources4
Beta strandi917 – 919Combined sources3
Beta strandi921 – 923Combined sources3
Beta strandi926 – 933Combined sources8
Helixi939 – 941Combined sources3
Helixi942 – 947Combined sources6
Beta strandi949 – 957Combined sources9
Beta strandi960 – 967Combined sources8
Beta strandi970 – 976Combined sources7
Beta strandi978 – 980Combined sources3
Beta strandi982 – 988Combined sources7
Beta strandi991 – 995Combined sources5
Beta strandi1003 – 1009Combined sources7
Beta strandi1011 – 1018Combined sources8
Beta strandi1021 – 1027Combined sources7
Beta strandi1038 – 1047Combined sources10
Beta strandi1054 – 1064Combined sources11
Helixi1068 – 1079Combined sources12
Beta strandi1089 – 1091Combined sources3
Beta strandi1093 – 1095Combined sources3
Beta strandi1097 – 1102Combined sources6
Helixi1103 – 1105Combined sources3
Beta strandi1108 – 1112Combined sources5
Beta strandi1116 – 1123Combined sources8
Beta strandi1145 – 1149Combined sources5
Turni1153 – 1155Combined sources3
Beta strandi1166 – 1173Combined sources8
Beta strandi1176 – 1183Combined sources8
Beta strandi1188 – 1192Combined sources5
Beta strandi1194 – 1198Combined sources5
Beta strandi1202 – 1205Combined sources4
Beta strandi1208 – 1211Combined sources4
Beta strandi1221 – 1231Combined sources11
Beta strandi1234 – 1246Combined sources13
Beta strandi1248 – 1250Combined sources3
Beta strandi1251 – 1260Combined sources10
Helixi1263 – 1266Combined sources4
Beta strandi1269 – 1271Combined sources3
Beta strandi1280 – 1283Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
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)DescriptionActionsGraphical viewLength
Sequence conflicti30T → M AA sequence (PubMed:3139097).Curated1
Sequence conflicti218R → G in CAA77991 (Ref. 2) Curated1
Sequence conflicti225A → S in CAA77991 (Ref. 2) Curated1
Sequence conflicti464S → R AA sequence (PubMed:3139097).Curated1

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.
PIRiA48940.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42782N.
IntActiP10844. 1 interactor.
MINTiMINT-1795550.
STRINGi445335.CBN_0875.

Chemistry databases

BindingDBiP10844.
ChEMBLiCHEMBL1075064.

Protein family/group databases

MEROPSiM27.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250958. Toxicity of botulinum toxin type B (BoNT/B).

Miscellaneous databases

EvolutionaryTraceiP10844.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
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]
ProtoNetiSearch...

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 2, 2016
This is version 151 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.