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Protein

Botulinum neurotoxin type A

Gene

botA

Organism
Clostridium botulinum
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of the three isoforms SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the '197-Gln-|-Arg-198' bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi223 – 2231Zinc; catalyticBy similarity
Active sitei224 – 2241By similarity
Metal bindingi227 – 2271Zinc; catalyticBy similarity

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

Names & Taxonomyi

Protein namesi
Recommended name:
Botulinum neurotoxin type A (EC:3.4.24.69)
Short name:
BoNT/A
Alternative name(s):
Bontoxilysin-A
Short name:
BOTOX
Cleaved into the following 2 chains:
Gene namesi
Name:botA
Synonyms:atx, bna
OrganismiClostridium botulinum
Taxonomic identifieri1491 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei627 – 64721HelicalSequence analysisAdd
BLAST
Transmembranei656 – 67621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

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 methionineiRemovedBy similarity
Chaini2 – 448447Botulinum neurotoxin A light chainPRO_0000029213Add
BLAST
Chaini449 – 1296848Botulinum neurotoxin A heavy chainPRO_0000029214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi430 ↔ 454Interchain (between light and heavy chains)By similarity
Disulfide bondi1235 ↔ 1280By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Disulfide-linked heterodimer of a light chain (L) and a heavy chain (H).By similarity

Protein-protein interaction databases

DIPiDIP-437N.

Structurei

Secondary structure

1
1296
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 238Combined sources
Beta strandi33 – 397Combined sources
Beta strandi42 – 487Combined sources
Beta strandi51 – 533Combined sources
Helixi54 – 563Combined sources
Turni75 – 784Combined sources
Helixi81 – 9919Combined sources
Helixi102 – 11312Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi133 – 1386Combined sources
Beta strandi144 – 1485Combined sources
Beta strandi150 – 1556Combined sources
Beta strandi164 – 1663Combined sources
Turni175 – 1773Combined sources
Beta strandi184 – 1874Combined sources
Beta strandi192 – 1987Combined sources
Helixi200 – 2034Combined sources
Beta strandi211 – 2144Combined sources
Helixi217 – 23216Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi254 – 2596Combined sources
Helixi260 – 2667Combined sources
Helixi268 – 2736Combined sources
Helixi276 – 29924Combined sources
Beta strandi305 – 3084Combined sources
Helixi310 – 32112Combined sources
Helixi335 – 34713Combined sources
Helixi351 – 3588Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi373 – 3753Combined sources
Turni381 – 3833Combined sources
Turni386 – 3883Combined sources
Beta strandi393 – 3953Combined sources
Helixi396 – 3983Combined sources
Helixi402 – 4043Combined sources
Turni406 – 4094Combined sources
Helixi410 – 4123Combined sources
Beta strandi414 – 4185Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E1HX-ray1.80A/C10-250[»]
B/D251-416[»]
2G7KX-ray2.80A/B3-426[»]
2G7NX-ray1.90A3-426[»]
2G7PX-ray2.30A/B3-426[»]
2G7QX-ray2.41A/B3-426[»]
ProteinModelPortaliQ45894.
SMRiQ45894. Positions 3-420.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ45894.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

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.

Sequencei

Sequence statusi: Complete.

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

Q45894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFVNKQFNY KDPVNGVDIA YIKIPNAGQM QPVKAFKIHN KIWVIPERDT
60 70 80 90 100
FTNPEEGDLN PPPEAKQVPV SYYDSTYLST DNEKDNYLKG VTKLFERIYS
110 120 130 140 150
TDLGRMLLTS IVRGIPFWGG STIDTELKVI DTNCINVIQP DGSYRSEELN
160 170 180 190 200
LVIIGPSADI IQFECKSFGH DVLNLTRNGY GSTQYIRFSP DFTFGFEESL
210 220 230 240 250
EVDTNPLLGA GKFATDPAVT LAHELIHAEH RLYGIAINPN RVFKVNTNAY
260 270 280 290 300
YEMSGLEVSF EELRTFGGHD AKFIDSLQEN EFRLYYYNKF KDVASTLNKA
310 320 330 340 350
KSIIGTTASL QYMKNVFKEK YLLSEDTSGK FSVDKLKFDK LYKMLTEIYT
360 370 380 390 400
EDNFVNFFKV INRKTYLNFD KAVFRINIVP DENYTIKDGF NLKGANLSTN
410 420 430 440 450
FNGQNTEINS RNFTRLKNFT GLFEFYKLLC VRGIIPFKTK SLDEGYNKAL
460 470 480 490 500
NDLCIKVNNW DLFFSPSEDN FTNDLDKVEE ITADTNIEAA EENISLDLIQ
510 520 530 540 550
QYYLTFDFDN EPENISIENL SSDIIGQLEP MPNIERFPNG KKYELDKYTM
560 570 580 590 600
FHYLRAQEFE HGDSRIILTN SAEEALLKPN VAYTFFSSKY VKKINKAVEA
610 620 630 640 650
FMFLNWAEEL VYDFTDETNE VTTMDKIADI TIIVPYIGPA LNIGNMLSKG
660 670 680 690 700
EFVEAIIFTG VVAMLEFIPE YALPVFGTFA IVSYIANKVL TVQTINNALS
710 720 730 740 750
KRNEKWDEVY KYTVTNWLAK VNTQIDLIRE KMKKALENQA EATKAIINYQ
760 770 780 790 800
YNQYTEEEKN NINFNIDDLS SKLNESINSA MININKFLDQ CSVSYLMNSM
810 820 830 840 850
IPYAVKRLKD FDASVRDVLL KYIYDNRGTL VLQVDRLKDE VNNTLSADIP
860 870 880 890 900
FQLSKYVDNK KLLSTFTEYI KNIVNTSILS IVYKKDDLID LSRYGAKINI
910 920 930 940 950
GDRVYYDSID KNQIKLINLE SSTIEVILKN AIVYNSMYEN FSTSFWIKIP
960 970 980 990 1000
KYFSKINLNN EYTIINCIEN NSGWKVSLNY GEIIWTLQDN KQNIQRVVFK
1010 1020 1030 1040 1050
YSQMVNISDY INRWIFVTIT NNRLTKSKIY INGRLIDQKP ISNLGNIHAS
1060 1070 1080 1090 1100
NKIMFKLDGC RDPRRYIMIK YFNLFDKELN EKEIKDLYDS QSNSGILKDF
1110 1120 1130 1140 1150
WGNYLQYDKP YYMLNLFDPN KYVDVNNIGI RGYMYLKGPR GSVVTTNIYL
1160 1170 1180 1190 1200
NSTLYEGTKF IIKKYASGNE DNIVRNNDRV YINVVVKNKE YRLATNASQA
1210 1220 1230 1240 1250
GVEKILSALE IPDVGNLSQV VVMKSKDDQG IRNKCKMNLQ DNNGNDIGFI
1260 1270 1280 1290
GFHLYDNIAK LVASNWYNRQ VGKASRTFGC SWEFIPVDDG WGESSL
Length:1,296
Mass (Da):149,411
Last modified:January 23, 2007 - v3
Checksum:i6F12E7BF28ED69D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73423 Genomic DNA. Translation: CAA51824.1.
X87974 Genomic DNA. Translation: CAA61234.1.
PIRiI40645.
RefSeqiWP_012703873.1. NZ_LFRC01000044.1.

Genome annotation databases

PATRICi19378373. VBICloBot91161_0812.

Cross-referencesi

Web resourcesi

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73423 Genomic DNA. Translation: CAA51824.1.
X87974 Genomic DNA. Translation: CAA61234.1.
PIRiI40645.
RefSeqiWP_012703873.1. NZ_LFRC01000044.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E1HX-ray1.80A/C10-250[»]
B/D251-416[»]
2G7KX-ray2.80A/B3-426[»]
2G7NX-ray1.90A3-426[»]
2G7PX-ray2.30A/B3-426[»]
2G7QX-ray2.41A/B3-426[»]
ProteinModelPortaliQ45894.
SMRiQ45894. Positions 3-420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-437N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

PATRICi19378373. VBICloBot91161_0812.

Miscellaneous databases

EvolutionaryTraceiQ45894.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiBXA2_CLOBO
AccessioniPrimary (citable) accession number: Q45894
Secondary accession number(s): P77780
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 130 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

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.