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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_CLOBU               Reviewed;        1251 AA.
P30995;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 122.
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 butyricum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1492;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 43181, and ATCC 43755;
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] OF 1-252.
STRAIN=BL6340;
PubMed=2033376; DOI=10.1099/00221287-137-3-519;
Fujii N., Kimura K., Murakami T., Indoh T., Tsuzuki K., Yokosawa N.,
Yashiki T., Oguma K.;
"Cloning of a DNA fragment encoding the 5'-terminus of the botulinum
type E toxin gene from Clostridium butyricum strain BL6340.";
J. Gen. Microbiol. 137:519-525(1991).
[3]
PROTEIN SEQUENCE OF 2-49.
STRAIN=5262;
Gimenez J., Foley J., Dasgupta B.R.;
"Neurotoxin type E from Clostridium botulinum and C. butyricum;
partial sequence and comparison.";
FASEB J. 2:A1750-A1750(1988).
-!- 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.
-!- 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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EMBL; X62088; CAA43998.1; -; Genomic_DNA.
EMBL; X53180; CAA37321.1; -; Genomic_DNA.
PIR; JH0256; JH0256.
ProteinModelPortal; P30995; -.
SMR; P30995; -.
MEROPS; M27.002; -.
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; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0051609; P:inhibition of neurotransmitter uptake; IEA:InterPro.
InterPro; IPR000395; Bot/tetX.
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;
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|Ref.3}.
CHAIN 2 422 Botulinum neurotoxin E light chain.
/FTId=PRO_0000029223.
CHAIN 423 1251 Botulinum neurotoxin E heavy chain.
/FTId=PRO_0000029224.
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 230 230 K -> M (in Ref. 2; CAA37321).
{ECO:0000305}.
SEQUENCE 1251 AA; 143397 MW; E8D7F180E9863581 CRC64;
MPTINSFNYN DPVNNRTILY IKPGGCQQFY KSFNIMKNIW IIPERNVIGT IPQDFLPPTS
LKNGDSSYYD PNYLQSDQEK DKFLKIVTKI FNRINDNLSG RILLEELSKA NPYLGNDNTP
DGDFIINDAS AVPIQFSNGS QSILLPNVII MGAEPDLFET NSSNISLRNN YMPSNHGFGS
IAIVTFSPEY SFRFKDNSMN EFIQDPALTL MHELIHSLHG LYGAKGITTK YTITQKQNPL
ITNIRGTNIE EFLTFGGTDL NIITSAQSND IYTNLLADYK KIASKLSKVQ VSNPLLNPYK
DVFEAKYGLD KDASGIYSVN INKFNDIFKK LYSFTEFDLA TKFQVKCRQT YIGQYKYFKL
SNLLNDSIYN ISEGYNINNL KVNFRGQNAN LNPRIITPIT GRGLVKKIIR FCKNIVSVKG
IRKSICIEIN NGELFFVASE NSYNDDNINT PKEIDDTVTS NNNYENDLDQ VILNFNSESA
PGLSDEKLNL TIQNDAYIPK YDSNGTSDIE QHDVNELNVF FYLDAQKVPE GENNVNLTSS
IDTALLEQPK IYTFFSSEFI NNVNKPVQAA LFVGWIQQVL VDFTTEANQK STVDKIADIS
IVVPYIGLAL NIGNEAQKGN FKDALELLGA GILLEFEPEL LIPTILVFTI KSFLGSSDNK
NKVIKAINNA LKERDEKWKE VYSFIVSNWM TKINTQFNKR KEQMYQALQN QVNALKAIIE
SKYNSYTLEE KNELTNKYDI EQIENELNQK VSIAMNNIDR FLTESSISYL MKLINEVKIN
KLREYDENVK TYLLDYIIKH GSILGESQQE LNSMVIDTLN NSIPFKLSSY TDDKILISYF
NKFFKRIKSS SVLNMRYKND KYVDTSGYDS NININGDVYK YPTNKNQFGI YNDKLSEVNI
SQNDYIIYDN KYKNFSISFW VRIPNYDNKI VNVNNEYTII NCMRDNNSGW KVSLNHNEII
WTLQDNSGIN QKLAFNYGNA NGISDYINKW IFVTITNDRL GDSKLYINGN LIDKKSILNL
GNIHVSDNIL FKIVNCSYTR YIGIRYFNIF DKELDETEIQ TLYNNEPNAN ILKDFWGNYL
LYDKEYYLLN VLKPNNFINR RTDSTLSINN IRSTILLANR LYSGIKVKIQ RVNNSSTNDN
LVRKNDQVYI NFVASKTHLL PLYADTATTN KEKTIKISSS GNRFNQVVVM NSVGNCTMNF
KNNNGNNIGL LGFKADTVVA STWYYTHMRD NTNSNGFFWN FISEEHGWQE K


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