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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)DescriptionActionsGraphical viewLength
Metal bindingi212Zinc; catalyticPROSITE-ProRule annotation1
Active sitei213PROSITE-ProRule annotation1
Metal bindingi216Zinc; 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-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 databases

ChEMBLiCHEMBL1697662.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000292212 – 422Botulinum neurotoxin E light chainAdd BLAST421
ChainiPRO_0000029222423 – 1251Botulinum neurotoxin E heavy chainAdd BLAST829

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactors.
STRINGi536233.CLO_2652.

Structurei

Secondary structure

11251
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 22Combined sources8
Beta strandi30 – 36Combined sources7
Beta strandi39 – 45Combined sources7
Helixi52 – 55Combined sources4
Turni61 – 64Combined sources4
Beta strandi65 – 67Combined sources3
Turni71 – 74Combined sources4
Helixi77 – 94Combined sources18
Helixi98 – 108Combined sources11
Turni128 – 130Combined sources3
Beta strandi132 – 135Combined sources4
Beta strandi141 – 144Combined sources4
Beta strandi147 – 152Combined sources6
Beta strandi161 – 164Combined sources4
Helixi168 – 170Combined sources3
Helixi173 – 175Combined sources3
Beta strandi176 – 178Combined sources3
Beta strandi182 – 185Combined sources4
Beta strandi190 – 195Combined sources6
Beta strandi196 – 199Combined sources4
Beta strandi201 – 203Combined sources3
Helixi206 – 221Combined sources16
Turni226 – 230Combined sources5
Beta strandi231 – 233Combined sources3
Turni235 – 239Combined sources5
Beta strandi240 – 242Combined sources3
Helixi249 – 255Combined sources7
Helixi257 – 262Combined sources6
Helixi265 – 287Combined sources23
Helixi294 – 296Combined sources3
Helixi297 – 306Combined sources10
Beta strandi309 – 311Combined sources3
Beta strandi313 – 315Combined sources3
Beta strandi317 – 319Combined sources3
Helixi321 – 333Combined sources13
Helixi336 – 343Combined sources8
Beta strandi357 – 361Combined sources5
Turni366 – 368Combined sources3
Turni371 – 373Combined sources3
Helixi378 – 387Combined sources10
Turni389 – 391Combined sources3
Helixi393 – 395Combined sources3
Turni400 – 403Combined sources4
Helixi404 – 408Combined sources5
Beta strandi418 – 420Combined sources3
Beta strandi422 – 430Combined sources9
Helixi431 – 433Combined sources3
Helixi468 – 472Combined sources5
Beta strandi505 – 507Combined sources3
Beta strandi510 – 513Combined sources4
Helixi519 – 525Combined sources7
Beta strandi536 – 539Combined sources4
Helixi541 – 546Combined sources6
Beta strandi550 – 552Combined sources3
Helixi557 – 560Combined sources4
Turni561 – 563Combined sources3
Helixi569 – 571Combined sources3
Helixi572 – 579Combined sources8
Helixi582 – 587Combined sources6
Beta strandi594 – 596Combined sources3
Helixi606 – 610Combined sources5
Helixi615 – 619Combined sources5
Helixi621 – 628Combined sources8
Helixi630 – 632Combined sources3
Helixi660 – 692Combined sources33
Helixi694 – 718Combined sources25
Turni719 – 721Combined sources3
Helixi722 – 724Combined sources3
Helixi728 – 731Combined sources4
Beta strandi740 – 743Combined sources4
Helixi744 – 779Combined sources36
Helixi781 – 799Combined sources19
Turni800 – 802Combined sources3
Helixi805 – 807Combined sources3
Helixi808 – 818Combined sources11
Beta strandi830 – 832Combined sources3
Beta strandi842 – 844Combined sources3
Beta strandi851 – 858Combined sources8
Beta strandi861 – 864Combined sources4
Beta strandi866 – 868Combined sources3
Beta strandi871 – 876Combined sources6
Beta strandi888 – 894Combined sources7
Beta strandi896 – 901Combined sources6
Turni904 – 906Combined sources3
Beta strandi916 – 922Combined sources7
Turni929 – 931Combined sources3
Beta strandi937 – 944Combined sources8
Turni945 – 947Combined sources3
Beta strandi948 – 955Combined sources8
Beta strandi958 – 964Combined sources7
Beta strandi966 – 968Combined sources3
Beta strandi970 – 976Combined sources7
Beta strandi991 – 997Combined sources7
Beta strandi1001 – 1007Combined sources7
Beta strandi1010 – 1016Combined sources7
Beta strandi1027 – 1035Combined sources9
Beta strandi1041 – 1052Combined sources12
Helixi1056 – 1063Combined sources8
Beta strandi1073 – 1079Combined sources7
Beta strandi1081 – 1083Combined sources3
Beta strandi1085 – 1092Combined sources8
Beta strandi1096 – 1100Combined sources5
Beta strandi1104 – 1111Combined sources8
Beta strandi1126 – 1133Combined sources8
Beta strandi1147 – 1155Combined sources9
Beta strandi1158 – 1165Combined sources8
Beta strandi1168 – 1177Combined sources10
Beta strandi1185 – 1194Combined sources10
Beta strandi1196 – 1202Combined sources7
Beta strandi1207 – 1214Combined sources8
Beta strandi1217 – 1222Combined sources6
Helixi1223 – 1226Combined sources4
Beta strandi1228 – 1230Combined sources3
Beta strandi1239 – 1242Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti177R → G in CAA44558 (PubMed:1541280).Curated1
Sequence conflicti198C → S (PubMed:1541280).Curated1
Sequence conflicti198C → S (PubMed:2160960).Curated1
Sequence conflicti340R → A in CAA44558 (PubMed:1541280).Curated1
Sequence conflicti773I → L (PubMed:1541280).Curated1
Sequence conflicti773I → L (PubMed:8408542).Curated1
Sequence conflicti963 – 964FE → LQ (PubMed:1541280).Curated2
Sequence conflicti963 – 964FE → LQ (PubMed:8408542).Curated2
Sequence conflicti967R → A (PubMed:1541280).Curated1
Sequence conflicti967R → A (PubMed:8408542).Curated1
Sequence conflicti1195N → NN in CAA44558 (PubMed:1541280).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

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...

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: November 2, 2016
This is version 147 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.