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Protein

Botulinum neurotoxin type E

Gene
N/A
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 catalyzes the hydrolysis of the 180-Arg-|-Ile-181 bond in SNAP-25.

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 bindingi212 – 2121Zinc; catalyticPROSITE-ProRule annotation
Active sitei213 – 2131PROSITE-ProRule annotation
Metal bindingi216 – 2161Zinc; catalyticPROSITE-ProRule annotation

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-5250992. Toxicity of botulinum toxin type E (BoNT/E).

Protein family/group databases

MEROPSiM27.002.
TCDBi1.C.8.1.3. the botulinum and tetanus toxin (btt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Botulinum neurotoxin type E (EC:3.4.24.69)
Short name:
BoNT/E
Alternative name(s):
Bontoxilysin-E
Cleaved into the following 2 chains:
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

ChEMBLiCHEMBL1697662.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 422421Botulinum neurotoxin E light chainPRO_0000029221Add
BLAST
Chaini423 – 1251829Botulinum neurotoxin E heavy chainPRO_0000029222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi412 ↔ 426Interchain (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.

Protein-protein interaction databases

DIPiDIP-46083N.
IntActiQ00496. 2 interactions.
STRINGi536233.CLO_2652.

Structurei

Secondary structure

1
1251
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 228Combined sources
Beta strandi30 – 367Combined sources
Beta strandi39 – 457Combined sources
Helixi52 – 554Combined sources
Turni61 – 644Combined sources
Beta strandi65 – 673Combined sources
Turni71 – 744Combined sources
Helixi77 – 9418Combined sources
Helixi98 – 10811Combined sources
Turni128 – 1303Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi141 – 1444Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi161 – 1644Combined sources
Helixi168 – 1703Combined sources
Helixi173 – 1753Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi182 – 1854Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi196 – 1994Combined sources
Beta strandi201 – 2033Combined sources
Helixi206 – 22116Combined sources
Turni226 – 2305Combined sources
Beta strandi231 – 2333Combined sources
Turni235 – 2395Combined sources
Beta strandi240 – 2423Combined sources
Helixi249 – 2557Combined sources
Helixi257 – 2626Combined sources
Helixi265 – 28723Combined sources
Helixi294 – 2963Combined sources
Helixi297 – 30610Combined sources
Beta strandi309 – 3113Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi317 – 3193Combined sources
Helixi321 – 33313Combined sources
Helixi336 – 3438Combined sources
Beta strandi357 – 3615Combined sources
Turni366 – 3683Combined sources
Turni371 – 3733Combined sources
Helixi378 – 38710Combined sources
Turni389 – 3913Combined sources
Helixi393 – 3953Combined sources
Turni400 – 4034Combined sources
Helixi404 – 4085Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi422 – 4309Combined sources
Helixi431 – 4333Combined sources
Helixi468 – 4725Combined sources
Beta strandi505 – 5073Combined sources
Beta strandi510 – 5134Combined sources
Helixi519 – 5257Combined sources
Beta strandi536 – 5394Combined sources
Helixi541 – 5466Combined sources
Beta strandi550 – 5523Combined sources
Helixi557 – 5604Combined sources
Turni561 – 5633Combined sources
Helixi569 – 5713Combined sources
Helixi572 – 5798Combined sources
Helixi582 – 5876Combined sources
Beta strandi594 – 5963Combined sources
Helixi606 – 6105Combined sources
Helixi615 – 6195Combined sources
Helixi621 – 6288Combined sources
Helixi630 – 6323Combined sources
Helixi660 – 69233Combined sources
Helixi694 – 71825Combined sources
Turni719 – 7213Combined sources
Helixi722 – 7243Combined sources
Helixi728 – 7314Combined sources
Beta strandi740 – 7434Combined sources
Helixi744 – 77936Combined sources
Helixi781 – 79919Combined sources
Turni800 – 8023Combined sources
Helixi805 – 8073Combined sources
Helixi808 – 81811Combined sources
Beta strandi830 – 8323Combined sources
Beta strandi842 – 8443Combined sources
Beta strandi851 – 8588Combined sources
Beta strandi861 – 8644Combined sources
Beta strandi866 – 8683Combined sources
Beta strandi871 – 8766Combined sources
Beta strandi888 – 8947Combined sources
Beta strandi896 – 9016Combined sources
Turni904 – 9063Combined sources
Beta strandi916 – 9227Combined sources
Turni929 – 9313Combined sources
Beta strandi937 – 9448Combined sources
Turni945 – 9473Combined sources
Beta strandi948 – 9558Combined sources
Beta strandi958 – 9647Combined sources
Beta strandi966 – 9683Combined sources
Beta strandi970 – 9767Combined sources
Beta strandi991 – 9977Combined sources
Beta strandi1001 – 10077Combined sources
Beta strandi1010 – 10167Combined sources
Beta strandi1027 – 10359Combined sources
Beta strandi1041 – 105212Combined sources
Helixi1056 – 10638Combined sources
Beta strandi1073 – 10797Combined sources
Beta strandi1081 – 10833Combined sources
Beta strandi1085 – 10928Combined sources
Beta strandi1096 – 11005Combined sources
Beta strandi1104 – 11118Combined sources
Beta strandi1126 – 11338Combined sources
Beta strandi1147 – 11559Combined sources
Beta strandi1158 – 11658Combined sources
Beta strandi1168 – 117710Combined sources
Beta strandi1185 – 119410Combined sources
Beta strandi1196 – 12027Combined sources
Beta strandi1207 – 12148Combined sources
Beta strandi1217 – 12226Combined sources
Helixi1223 – 12264Combined sources
Beta strandi1228 – 12303Combined sources
Beta strandi1239 – 12424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3AX-ray2.16A/B2-422[»]
1T3CX-ray1.90A/B2-422[»]
1ZKWX-ray2.17A/B2-421[»]
1ZKXX-ray2.52A/B2-421[»]
1ZL5X-ray2.60A/B2-421[»]
1ZL6X-ray2.40A/B2-421[»]
1ZN3X-ray2.60A/B2-421[»]
3FFZX-ray2.65A/B1-1251[»]
DisProtiDP00732.
ProteinModelPortaliQ00496.
SMRiQ00496. Positions 2-412.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00496.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

Keywords - Domaini

Transmembrane

Phylogenomic databases

KOiK06011.

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.

Q00496-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKINSFNYN DPVNDRTILY IKPGGCQEFY KSFNIMKNIW IIPERNVIGT
60 70 80 90 100
TPQDFHPPTS LKNGDSSYYD PNYLQSDEEK DRFLKIVTKI FNRINNNLSG
110 120 130 140 150
GILLEELSKA NPYLGNDNTP DNQFHIGDAS AVEIKFSNGS QDILLPNVII
160 170 180 190 200
MGAEPDLFET NSSNISLRNN YMPSNHRFGS IAIVTFSPEY SFRFNDNCMN
210 220 230 240 250
EFIQDPALTL MHELIHSLHG LYGAKGITTK YTITQKQNPL ITNIRGTNIE
260 270 280 290 300
EFLTFGGTDL NIITSAQSND IYTNLLADYK KIASKLSKVQ VSNPLLNPYK
310 320 330 340 350
DVFEAKYGLD KDASGIYSVN INKFNDIFKK LYSFTEFDLR TKFQVKCRQT
360 370 380 390 400
YIGQYKYFKL SNLLNDSIYN ISEGYNINNL KVNFRGQNAN LNPRIITPIT
410 420 430 440 450
GRGLVKKIIR FCKNIVSVKG IRKSICIEIN NGELFFVASE NSYNDDNINT
460 470 480 490 500
PKEIDDTVTS NNNYENDLDQ VILNFNSESA PGLSDEKLNL TIQNDAYIPK
510 520 530 540 550
YDSNGTSDIE QHDVNELNVF FYLDAQKVPE GENNVNLTSS IDTALLEQPK
560 570 580 590 600
IYTFFSSEFI NNVNKPVQAA LFVSWIQQVL VDFTTEANQK STVDKIADIS
610 620 630 640 650
IVVPYIGLAL NIGNEAQKGN FKDALELLGA GILLEFEPEL LIPTILVFTI
660 670 680 690 700
KSFLGSSDNK NKVIKAINNA LKERDEKWKE VYSFIVSNWM TKINTQFNKR
710 720 730 740 750
KEQMYQALQN QVNAIKTIIE SKYNSYTLEE KNELTNKYDI KQIENELNQK
760 770 780 790 800
VSIAMNNIDR FLTESSISYL MKIINEVKIN KLREYDENVK TYLLNYIIQH
810 820 830 840 850
GSILGESQQE LNSMVTDTLN NSIPFKLSSY TDDKILISYF NKFFKRIKSS
860 870 880 890 900
SVLNMRYKND KYVDTSGYDS NININGDVYK YPTNKNQFGI YNDKLSEVNI
910 920 930 940 950
SQNDYIIYDN KYKNFSISFW VRIPNYDNKI VNVNNEYTII NCMRDNNSGW
960 970 980 990 1000
KVSLNHNEII WTFEDNRGIN QKLAFNYGNA NGISDYINKW IFVTITNDRL
1010 1020 1030 1040 1050
GDSKLYINGN LIDQKSILNL GNIHVSDNIL FKIVNCSYTR YIGIRYFNIF
1060 1070 1080 1090 1100
DKELDETEIQ TLYSNEPNTN ILKDFWGNYL LYDKEYYLLN VLKPNNFIDR
1110 1120 1130 1140 1150
RKDSTLSINN IRSTILLANR LYSGIKVKIQ RVNNSSTNDN LVRKNDQVYI
1160 1170 1180 1190 1200
NFVASKTHLF PLYADTATTN KEKTIKISSS GNRFNQVVVM NSVGNCTMNF
1210 1220 1230 1240 1250
KNNNGNNIGL LGFKADTVVA STWYYTHMRD HTNSNGCFWN FISEEHGWQE

K
Length:1,251
Mass (Da):143,844
Last modified:January 23, 2007 - v2
Checksum:iB05AA65FF1B30362
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1771R → G in CAA44558 (PubMed:1541280).Curated
Sequence conflicti198 – 1981C → S (PubMed:1541280).Curated
Sequence conflicti198 – 1981C → S (PubMed:2160960).Curated
Sequence conflicti340 – 3401R → A in CAA44558 (PubMed:1541280).Curated
Sequence conflicti773 – 7731I → L (PubMed:1541280).Curated
Sequence conflicti773 – 7731I → L (PubMed:8408542).Curated
Sequence conflicti963 – 9642FE → LQ (PubMed:1541280).Curated
Sequence conflicti963 – 9642FE → LQ (PubMed:8408542).Curated
Sequence conflicti967 – 9671R → A (PubMed:1541280).Curated
Sequence conflicti967 – 9671R → A (PubMed:8408542).Curated
Sequence conflicti1195 – 11951N → NN in CAA44558 (PubMed:1541280).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62089 Genomic DNA. Translation: CAA43999.1.
X62683 Genomic DNA. Translation: CAA44558.1.
X70815 Genomic DNA. Translation: CAA50146.1.
PIRiS08575.
S21178.
RefSeqiWP_003372387.1. NZ_LHUM01000023.1.

Genome annotation databases

KEGGiag:CAA43999.

Cross-referencesi

Web resourcesi

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62089 Genomic DNA. Translation: CAA43999.1.
X62683 Genomic DNA. Translation: CAA44558.1.
X70815 Genomic DNA. Translation: CAA50146.1.
PIRiS08575.
S21178.
RefSeqiWP_003372387.1. NZ_LHUM01000023.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3AX-ray2.16A/B2-422[»]
1T3CX-ray1.90A/B2-422[»]
1ZKWX-ray2.17A/B2-421[»]
1ZKXX-ray2.52A/B2-421[»]
1ZL5X-ray2.60A/B2-421[»]
1ZL6X-ray2.40A/B2-421[»]
1ZN3X-ray2.60A/B2-421[»]
3FFZX-ray2.65A/B1-1251[»]
DisProtiDP00732.
ProteinModelPortaliQ00496.
SMRiQ00496. Positions 2-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46083N.
IntActiQ00496. 2 interactions.
STRINGi536233.CLO_2652.

Chemistry

ChEMBLiCHEMBL1697662.

Protein family/group databases

MEROPSiM27.002.
TCDBi1.C.8.1.3. the botulinum and tetanus toxin (btt) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA43999.

Phylogenomic databases

KOiK06011.

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250992. Toxicity of botulinum toxin type E (BoNT/E).

Miscellaneous databases

EvolutionaryTraceiQ00496.

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...

Publicationsi

  1. "Sequences of the botulinal neurotoxin E derived from Clostridium botulinum type E (strain Beluga) and Clostridium butyricum (strains ATCC 43181 and ATCC 43755)."
    Poulet S., Hauser D., Quanz M., Niemann H., Popoff M.R.
    Biochem. Biophys. Res. Commun. 183:107-113(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Type E / Beluga.
  2. "The complete amino acid sequence of the Clostridium botulinum type-E neurotoxin, derived by nucleotide-sequence analysis of the encoding gene."
    Whelan S.M., Elmore M.J., Bodsworth N.J., Atkinson T., Minton N.P.
    Eur. J. Biochem. 204:657-667(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins."
    Binz T., Kurazono H., Wille M., Frevert J., Wernars K., Niemann H.
    J. Biol. Chem. 265:9153-9158(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
  4. "Partial amino acid sequences of botulinum neurotoxins types B and E."
    Schmidt J.J., Sathyamoorthy V., Dasgupta B.R.
    Arch. Biochem. Biophys. 238:544-548(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-14.
  5. "Botulinum neurotoxin type E fragmented with endoproteinase Lys-C reveals the site trypsin nicks and homology with tetanus neurotoxin."
    Gimenez J.A., Dasgupta B.R.
    Biochimie 72:213-217(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 420-427.
  6. "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 616-982.
    Strain: Type E / Hazen 36208.
  7. "Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds."
    Schiavo G., Santtuci A., Dasgupta B.R., Mehta P.P., Jontes J., Benfenati F., Wilson M.C., Montecucco C.
    FEBS Lett. 335:99-103(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF SUBSTRATE.
  8. "Proteolysis of SNAP-25 by types E and A botulinal neurotoxins."
    Binz T., Blasi J., Yamasaki S., Baumeister A., Link E., Suedhof T.C., Jahn R., Niemann H.
    J. Biol. Chem. 269:1617-1620(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF SUBSTRATE.

Entry informationi

Entry nameiBXE_CLOBO
AccessioniPrimary (citable) accession number: Q00496
Secondary accession number(s): Q45862
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 144 of the entry and version 2 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.