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Botulinum neurotoxin type E (BoNT/E) (EC 3.4.24.69) (Bontoxilysin-E) [Cleaved into: Botulinum neurotoxin E light chain; Botulinum neurotoxin E heavy chain]

 BXE_CLOBO               Reviewed;        1251 AA.
Q00496; Q45862;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 158.
RecName: Full=Botulinum neurotoxin type E;
Short=BoNT/E;
EC=3.4.24.69;
AltName: Full=Bontoxilysin-E;
Contains:
RecName: Full=Botulinum neurotoxin E light chain;
Contains:
RecName: Full=Botulinum neurotoxin E heavy chain;
Flags: Precursor;
Clostridium botulinum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1491;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Beluga / Type E;
PubMed=1543481; DOI=10.1016/0006-291X(92)91615-W;
Poulet S., Hauser D., Quanz M., Niemann H., Popoff M.R.;
"Sequences of the botulinal neurotoxin E derived from Clostridium
botulinum type E (strain Beluga) and Clostridium butyricum (strains
ATCC 43181 and ATCC 43755).";
Biochem. Biophys. Res. Commun. 183:107-113(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1541280; DOI=10.1111/j.1432-1033.1992.tb16679.x;
Whelan S.M., Elmore M.J., Bodsworth N.J., Atkinson T., Minton N.P.;
"The complete amino acid sequence of the Clostridium botulinum type-E
neurotoxin, derived by nucleotide-sequence analysis of the encoding
gene.";
Eur. J. Biochem. 204:657-667(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
PubMed=2160960;
Binz T., Kurazono H., Wille M., Frevert J., Wernars K., Niemann H.;
"The complete sequence of botulinum neurotoxin type A and comparison
with other clostridial neurotoxins.";
J. Biol. Chem. 265:9153-9158(1990).
[4]
PROTEIN SEQUENCE OF 2-14.
PubMed=3888113; DOI=10.1016/0003-9861(85)90198-5;
Schmidt J.J., Sathyamoorthy V., Dasgupta B.R.;
"Partial amino acid sequences of botulinum neurotoxins types B and
E.";
Arch. Biochem. Biophys. 238:544-548(1985).
[5]
PROTEIN SEQUENCE OF 420-427.
PubMed=2116911; DOI=10.1016/0300-9084(90)90075-R;
Gimenez J.A., Dasgupta B.R.;
"Botulinum neurotoxin type E fragmented with endoproteinase Lys-C
reveals the site trypsin nicks and homology with tetanus neurotoxin.";
Biochimie 72:213-217(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 616-982.
STRAIN=Hazen 36208 / Type E;
PubMed=8408542;
Campbell K.D., Collins M.D., East A.K.;
"Gene probes for identification of the botulinal neurotoxin gene and
specific identification of neurotoxin types B, E, and F.";
J. Clin. Microbiol. 31:2255-2262(1993).
[7]
IDENTIFICATION OF SUBSTRATE.
PubMed=8243676; DOI=10.1016/0014-5793(93)80448-4;
Schiavo G., Santtuci A., Dasgupta B.R., Mehta P.P., Jontes J.,
Benfenati F., Wilson M.C., Montecucco C.;
"Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct
COOH-terminal peptide bonds.";
FEBS Lett. 335:99-103(1993).
[8]
IDENTIFICATION OF SUBSTRATE.
PubMed=8294407;
Binz T., Blasi J., Yamasaki S., Baumeister A., Link E., Suedhof T.C.,
Jahn R., Niemann H.;
"Proteolysis of SNAP-25 by types E and A botulinal neurotoxins.";
J. Biol. Chem. 269:1617-1620(1994).
-!- FUNCTION: 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 ACTIVITY: Limited hydrolysis of proteins of the
neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No
detected action on small molecule substrates.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: 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.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin E light chain:
Secreted. Host cytoplasm, host cytosol.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin E heavy chain:
Secreted. Host cell junction, host synapse, host presynaptic cell
membrane {ECO:0000305}.
-!- MISCELLANEOUS: There are seven antigenically distinct forms of
botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
-!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial
Neurotoxins;
URL="https://botdb.abcc.ncifcrf.gov/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X62089; CAA43999.1; -; Genomic_DNA.
EMBL; X62683; CAA44558.1; -; Genomic_DNA.
EMBL; X70815; CAA50146.1; -; Genomic_DNA.
PIR; S08575; S08575.
PIR; S21178; S21178.
RefSeq; WP_003372387.1; NZ_MWJG01000001.1.
PDB; 1T3A; X-ray; 2.16 A; A/B=2-422.
PDB; 1T3C; X-ray; 1.90 A; A/B=2-422.
PDB; 1ZKW; X-ray; 2.17 A; A/B=2-421.
PDB; 1ZKX; X-ray; 2.52 A; A/B=2-421.
PDB; 1ZL5; X-ray; 2.60 A; A/B=2-421.
PDB; 1ZL6; X-ray; 2.40 A; A/B=2-421.
PDB; 1ZN3; X-ray; 2.60 A; A/B=2-421.
PDB; 3FFZ; X-ray; 2.65 A; A/B=1-1251.
PDBsum; 1T3A; -.
PDBsum; 1T3C; -.
PDBsum; 1ZKW; -.
PDBsum; 1ZKX; -.
PDBsum; 1ZL5; -.
PDBsum; 1ZL6; -.
PDBsum; 1ZN3; -.
PDBsum; 3FFZ; -.
DisProt; DP00732; -.
ProteinModelPortal; Q00496; -.
SMR; Q00496; -.
DIP; DIP-46083N; -.
IntAct; Q00496; 4.
MINT; Q00496; -.
BindingDB; Q00496; -.
ChEMBL; CHEMBL1697662; -.
MEROPS; M27.002; -.
TCDB; 1.C.8.1.3; the botulinum and tetanus toxin (btt) family.
KEGG; ag:CAA43999; -.
KO; K06011; -.
BRENDA; 3.4.24.69; 1462.
Reactome; R-HSA-5250992; Toxicity of botulinum toxin type E (BoNT/E).
EvolutionaryTrace; Q00496; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
GO; GO:0044156; C:host cell junction; IEA:UniProtKB-KW.
GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome.
GO; GO:0008320; F:protein transmembrane transporter activity; EXP:Reactome.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0051609; P:inhibition of neurotransmitter uptake; IEA:InterPro.
Gene3D; 1.20.1120.10; -; 1.
InterPro; IPR000395; Bot/tetX_LC.
InterPro; IPR036248; Clostridium_toxin_transloc.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
InterPro; IPR013104; Toxin_rcpt-bd_C.
InterPro; IPR012928; Toxin_rcpt-bd_N.
InterPro; IPR012500; Toxin_trans.
Pfam; PF01742; Peptidase_M27; 1.
Pfam; PF07951; Toxin_R_bind_C; 1.
Pfam; PF07953; Toxin_R_bind_N; 1.
Pfam; PF07952; Toxin_trans; 1.
PRINTS; PR00760; BONTOXILYSIN.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF50386; SSF50386; 1.
SUPFAM; SSF58091; SSF58091; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Host cell junction; Host cell membrane; Host cytoplasm; Host membrane;
Host synapse; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Neurotoxin; Protease; Secreted; Toxin; Transmembrane; Virulence; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3888113}.
CHAIN 2 422 Botulinum neurotoxin E light chain.
/FTId=PRO_0000029221.
CHAIN 423 1251 Botulinum neurotoxin E heavy chain.
/FTId=PRO_0000029222.
ACT_SITE 213 213 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 212 212 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 216 216 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
DISULFID 412 426 Interchain (between light and heavy
chains). {ECO:0000305}.
CONFLICT 177 177 R -> G (in Ref. 2; CAA44558).
{ECO:0000305}.
CONFLICT 198 198 C -> S (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 340 340 R -> A (in Ref. 2; CAA44558).
{ECO:0000305}.
CONFLICT 773 773 I -> L (in Ref. 2 and 6). {ECO:0000305}.
CONFLICT 963 964 FE -> LQ (in Ref. 2 and 6).
{ECO:0000305}.
CONFLICT 967 967 R -> A (in Ref. 2 and 6). {ECO:0000305}.
CONFLICT 1195 1195 N -> NN (in Ref. 2; CAA44558).
{ECO:0000305}.
STRAND 15 22 {ECO:0000244|PDB:1T3C}.
STRAND 30 36 {ECO:0000244|PDB:1T3C}.
STRAND 39 45 {ECO:0000244|PDB:1T3C}.
HELIX 52 55 {ECO:0000244|PDB:1T3C}.
TURN 61 64 {ECO:0000244|PDB:1T3C}.
STRAND 65 67 {ECO:0000244|PDB:1ZL5}.
TURN 71 74 {ECO:0000244|PDB:1T3C}.
HELIX 77 94 {ECO:0000244|PDB:1T3C}.
HELIX 98 108 {ECO:0000244|PDB:1T3C}.
TURN 128 130 {ECO:0000244|PDB:1T3C}.
STRAND 132 135 {ECO:0000244|PDB:1T3C}.
STRAND 141 144 {ECO:0000244|PDB:1T3C}.
STRAND 147 152 {ECO:0000244|PDB:1T3C}.
STRAND 161 164 {ECO:0000244|PDB:1T3C}.
HELIX 168 170 {ECO:0000244|PDB:1T3C}.
HELIX 173 175 {ECO:0000244|PDB:1T3C}.
STRAND 176 178 {ECO:0000244|PDB:1T3C}.
STRAND 182 185 {ECO:0000244|PDB:1T3C}.
STRAND 190 195 {ECO:0000244|PDB:1T3C}.
STRAND 196 199 {ECO:0000244|PDB:3FFZ}.
STRAND 201 203 {ECO:0000244|PDB:1T3C}.
HELIX 206 221 {ECO:0000244|PDB:1T3C}.
TURN 226 230 {ECO:0000244|PDB:1T3C}.
STRAND 231 233 {ECO:0000244|PDB:1T3A}.
TURN 235 239 {ECO:0000244|PDB:1T3C}.
STRAND 240 242 {ECO:0000244|PDB:1ZKW}.
HELIX 249 255 {ECO:0000244|PDB:1T3C}.
HELIX 257 262 {ECO:0000244|PDB:1T3C}.
HELIX 265 287 {ECO:0000244|PDB:1T3C}.
HELIX 294 296 {ECO:0000244|PDB:1T3C}.
HELIX 297 306 {ECO:0000244|PDB:1T3C}.
STRAND 309 311 {ECO:0000244|PDB:1T3C}.
STRAND 313 315 {ECO:0000244|PDB:3FFZ}.
STRAND 317 319 {ECO:0000244|PDB:1T3C}.
HELIX 321 333 {ECO:0000244|PDB:1T3C}.
HELIX 336 343 {ECO:0000244|PDB:1T3C}.
STRAND 357 361 {ECO:0000244|PDB:1T3C}.
TURN 366 368 {ECO:0000244|PDB:1T3C}.
TURN 371 373 {ECO:0000244|PDB:1T3C}.
HELIX 378 387 {ECO:0000244|PDB:1T3C}.
TURN 389 391 {ECO:0000244|PDB:1T3C}.
HELIX 393 395 {ECO:0000244|PDB:1T3C}.
TURN 400 403 {ECO:0000244|PDB:1T3C}.
HELIX 404 408 {ECO:0000244|PDB:1T3C}.
STRAND 418 420 {ECO:0000244|PDB:3FFZ}.
STRAND 422 430 {ECO:0000244|PDB:3FFZ}.
HELIX 431 433 {ECO:0000244|PDB:3FFZ}.
HELIX 468 472 {ECO:0000244|PDB:3FFZ}.
STRAND 505 507 {ECO:0000244|PDB:3FFZ}.
STRAND 510 513 {ECO:0000244|PDB:3FFZ}.
HELIX 519 525 {ECO:0000244|PDB:3FFZ}.
STRAND 536 539 {ECO:0000244|PDB:3FFZ}.
HELIX 541 546 {ECO:0000244|PDB:3FFZ}.
STRAND 550 552 {ECO:0000244|PDB:3FFZ}.
HELIX 557 560 {ECO:0000244|PDB:3FFZ}.
TURN 561 563 {ECO:0000244|PDB:3FFZ}.
HELIX 569 571 {ECO:0000244|PDB:3FFZ}.
HELIX 572 579 {ECO:0000244|PDB:3FFZ}.
HELIX 582 587 {ECO:0000244|PDB:3FFZ}.
STRAND 594 596 {ECO:0000244|PDB:3FFZ}.
HELIX 606 610 {ECO:0000244|PDB:3FFZ}.
HELIX 615 619 {ECO:0000244|PDB:3FFZ}.
HELIX 621 628 {ECO:0000244|PDB:3FFZ}.
HELIX 630 632 {ECO:0000244|PDB:3FFZ}.
HELIX 660 692 {ECO:0000244|PDB:3FFZ}.
HELIX 694 718 {ECO:0000244|PDB:3FFZ}.
TURN 719 721 {ECO:0000244|PDB:3FFZ}.
HELIX 722 724 {ECO:0000244|PDB:3FFZ}.
HELIX 728 731 {ECO:0000244|PDB:3FFZ}.
STRAND 740 743 {ECO:0000244|PDB:3FFZ}.
HELIX 744 779 {ECO:0000244|PDB:3FFZ}.
HELIX 781 799 {ECO:0000244|PDB:3FFZ}.
TURN 800 802 {ECO:0000244|PDB:3FFZ}.
HELIX 805 807 {ECO:0000244|PDB:3FFZ}.
HELIX 808 818 {ECO:0000244|PDB:3FFZ}.
STRAND 830 832 {ECO:0000244|PDB:3FFZ}.
STRAND 842 844 {ECO:0000244|PDB:3FFZ}.
STRAND 851 858 {ECO:0000244|PDB:3FFZ}.
STRAND 861 864 {ECO:0000244|PDB:3FFZ}.
STRAND 866 868 {ECO:0000244|PDB:3FFZ}.
STRAND 871 876 {ECO:0000244|PDB:3FFZ}.
STRAND 888 894 {ECO:0000244|PDB:3FFZ}.
STRAND 896 901 {ECO:0000244|PDB:3FFZ}.
TURN 904 906 {ECO:0000244|PDB:3FFZ}.
STRAND 916 922 {ECO:0000244|PDB:3FFZ}.
TURN 929 931 {ECO:0000244|PDB:3FFZ}.
STRAND 937 944 {ECO:0000244|PDB:3FFZ}.
TURN 945 947 {ECO:0000244|PDB:3FFZ}.
STRAND 948 955 {ECO:0000244|PDB:3FFZ}.
STRAND 958 964 {ECO:0000244|PDB:3FFZ}.
STRAND 966 968 {ECO:0000244|PDB:3FFZ}.
STRAND 970 976 {ECO:0000244|PDB:3FFZ}.
STRAND 991 997 {ECO:0000244|PDB:3FFZ}.
STRAND 1001 1007 {ECO:0000244|PDB:3FFZ}.
STRAND 1010 1016 {ECO:0000244|PDB:3FFZ}.
STRAND 1027 1035 {ECO:0000244|PDB:3FFZ}.
STRAND 1041 1052 {ECO:0000244|PDB:3FFZ}.
HELIX 1056 1063 {ECO:0000244|PDB:3FFZ}.
STRAND 1073 1079 {ECO:0000244|PDB:3FFZ}.
STRAND 1081 1083 {ECO:0000244|PDB:3FFZ}.
STRAND 1085 1092 {ECO:0000244|PDB:3FFZ}.
STRAND 1096 1100 {ECO:0000244|PDB:3FFZ}.
STRAND 1104 1111 {ECO:0000244|PDB:3FFZ}.
STRAND 1126 1133 {ECO:0000244|PDB:3FFZ}.
STRAND 1147 1155 {ECO:0000244|PDB:3FFZ}.
STRAND 1158 1165 {ECO:0000244|PDB:3FFZ}.
STRAND 1168 1177 {ECO:0000244|PDB:3FFZ}.
STRAND 1185 1194 {ECO:0000244|PDB:3FFZ}.
STRAND 1196 1202 {ECO:0000244|PDB:3FFZ}.
STRAND 1207 1214 {ECO:0000244|PDB:3FFZ}.
STRAND 1217 1222 {ECO:0000244|PDB:3FFZ}.
HELIX 1223 1226 {ECO:0000244|PDB:3FFZ}.
STRAND 1228 1230 {ECO:0000244|PDB:3FFZ}.
STRAND 1239 1242 {ECO:0000244|PDB:3FFZ}.
SEQUENCE 1251 AA; 143844 MW; B05AA65FF1B30362 CRC64;
MPKINSFNYN DPVNDRTILY IKPGGCQEFY KSFNIMKNIW IIPERNVIGT TPQDFHPPTS
LKNGDSSYYD PNYLQSDEEK DRFLKIVTKI FNRINNNLSG GILLEELSKA NPYLGNDNTP
DNQFHIGDAS AVEIKFSNGS QDILLPNVII MGAEPDLFET NSSNISLRNN YMPSNHRFGS
IAIVTFSPEY SFRFNDNCMN EFIQDPALTL MHELIHSLHG LYGAKGITTK YTITQKQNPL
ITNIRGTNIE EFLTFGGTDL NIITSAQSND IYTNLLADYK KIASKLSKVQ VSNPLLNPYK
DVFEAKYGLD KDASGIYSVN INKFNDIFKK LYSFTEFDLR TKFQVKCRQT YIGQYKYFKL
SNLLNDSIYN ISEGYNINNL KVNFRGQNAN LNPRIITPIT GRGLVKKIIR FCKNIVSVKG
IRKSICIEIN NGELFFVASE NSYNDDNINT PKEIDDTVTS NNNYENDLDQ VILNFNSESA
PGLSDEKLNL TIQNDAYIPK YDSNGTSDIE QHDVNELNVF FYLDAQKVPE GENNVNLTSS
IDTALLEQPK IYTFFSSEFI NNVNKPVQAA LFVSWIQQVL VDFTTEANQK STVDKIADIS
IVVPYIGLAL NIGNEAQKGN FKDALELLGA GILLEFEPEL LIPTILVFTI KSFLGSSDNK
NKVIKAINNA LKERDEKWKE VYSFIVSNWM TKINTQFNKR KEQMYQALQN QVNAIKTIIE
SKYNSYTLEE KNELTNKYDI KQIENELNQK VSIAMNNIDR FLTESSISYL MKIINEVKIN
KLREYDENVK TYLLNYIIQH GSILGESQQE LNSMVTDTLN NSIPFKLSSY TDDKILISYF
NKFFKRIKSS SVLNMRYKND KYVDTSGYDS NININGDVYK YPTNKNQFGI YNDKLSEVNI
SQNDYIIYDN KYKNFSISFW VRIPNYDNKI VNVNNEYTII NCMRDNNSGW KVSLNHNEII
WTFEDNRGIN QKLAFNYGNA NGISDYINKW IFVTITNDRL GDSKLYINGN LIDQKSILNL
GNIHVSDNIL FKIVNCSYTR YIGIRYFNIF DKELDETEIQ TLYSNEPNTN ILKDFWGNYL
LYDKEYYLLN VLKPNNFIDR RKDSTLSINN IRSTILLANR LYSGIKVKIQ RVNNSSTNDN
LVRKNDQVYI NFVASKTHLF PLYADTATTN KEKTIKISSS GNRFNQVVVM NSVGNCTMNF
KNNNGNNIGL LGFKADTVVA STWYYTHMRD HTNSNGCFWN FISEEHGWQE K


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