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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.
18-JUL-2018, entry version 126.
RecName: Full=Botulinum neurotoxin type E;
Short=BoNT/E;
AltName: Full=Bontoxilysin-E;
Contains:
RecName: Full=Botulinum neurotoxin E light chain;
Short=LC;
EC=3.4.24.69;
Contains:
RecName: Full=Botulinum neurotoxin E heavy chain;
Short=HC;
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).
[4]
FUNCTION (BOTULINUM NEUROTOXIN E HEAVY CHAIN), GANGLIOSIDE-BINDING,
AND MUTAGENESIS OF LYS-1093; LYS-1214 AND ARG-1229.
STRAIN=ATCC 43181, and ATCC 43755;
PubMed=21849494; DOI=10.1074/jbc.M111.272054;
Benson M.A., Fu Z., Kim J.J., Baldwin M.R.;
"Unique ganglioside recognition strategies for clostridial
neurotoxins.";
J. Biol. Chem. 286:34015-34022(2011).
-!- FUNCTION: Botulinum neurotoxin type E: Botulinum toxin causes
flaccid paralysis by inhibiting neurotransmitter (acetylcholine)
release from the presynaptic membranes of nerve terminals of
eukaryotic host skeletal and autonomic nervous system, with
frequent heart or respiratory failure. Precursor of botulinum
neurotoxin E which has 2 coreceptors; complex polysialylated
gangliosides found on neural tissue and specific membrane-anchored
proteins found in synaptic vesicles. Receptor proteins are exposed
on host presynaptic cell membrane during neurotransmitter release,
when the toxin heavy chain (HC) binds to them. Upon synaptic
vesicle recycling the toxin is taken up via the endocytic pathway.
When the pH of the toxin-containing endosome drops a structural
rearrangement occurs so that the N-terminus of the HC forms pores
that allows the light chain (LC) to translocate into the cytosol.
Once in the cytosol the disulfide bond linking the 2 subunits is
reduced and LC cleaves its target protein on synaptic vesicles,
preventing their fusion with the cytoplasmic membrane and thus
neurotransmitter release (By similarity).
{ECO:0000250|UniProtKB:Q00496}.
-!- FUNCTION: Botulinum neurotoxin E light chain: Has proteolytic
activity. After translocation into the eukaryotic host cytosol, LC
hydrolyzes the '180-Arg-|-Ile-181' bond in SNAP25, blocking
neurotransmitter release (By similarity).
{ECO:0000250|UniProtKB:Q00496}.
-!- FUNCTION: Botulinum neurotoxin E heavy chain: Responsible for host
epithelial cell transcytosis, host nerve cell targeting and
translocation of light chain (LC) into host cytosol. Composed of 3
subdomains; the translocation domain (TD), and N-terminus and C-
terminus of the receptor-binding domain (RBD). The RBD is
responsible for the adherence of the toxin to the cell surface. It
simultaneously recognizes 2 coreceptors; host polysialated
gangliosides and the receptor proteins SV2A and SV2B in close
proximity on host synaptic vesicles. Interaction with SV2 proteins
requires SV2 glycosylation. The N-terminus of the TD wraps an
extended belt around the perimeter of the LC, protecting Zn(2+) in
the active site; it may also prevent premature LC dissociation
from the translocation channel and protect toxin prior to
translocation (By similarity). The TD inserts into synaptic
vesicle membrane to allow translocation into the host cytosol (By
similarity). Binds ganglioside GD1a in vitro (PubMed:21849494).
{ECO:0000250|UniProtKB:Q00496, ECO:0000269|PubMed:21849494}.
-!- CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the
neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No
detected action on small molecule substrates.
{ECO:0000250|UniProtKB:Q00496}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q00496};
Note=Binds 1 zinc ion per subunit (By similarity).
{ECO:0000250|UniProtKB:Q00496};
-!- SUBUNIT: Heterodimer; disulfide-linked heterodimer of a light
chain (LC) and a heavy chain (HC). The LC has the
proteolytic/pharmacological activity, while the N- and C-terminal
of the HC mediate channel formation and toxin binding,
respectively. Interacts with host synaptic vesicle glycoproteins
SV2A and SV2B which probably serve as coreceptors.
{ECO:0000250|UniProtKB:Q00496}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin type E: Secreted
{ECO:0000250|UniProtKB:Q00496}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin E light chain:
Secreted. Host cytoplasm, host cytosol
{ECO:0000250|UniProtKB:Q00496}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin E heavy chain:
Secreted. Host cell junction, host synapse, host presynaptic cell
membrane {ECO:0000250|UniProtKB:Q00496}. Host cytoplasmic vesicle,
host secretory vesicle, host synaptic vesicle membrane
{ECO:0000250|UniProtKB:P0DPI0}; Multi-pass membrane protein
{ECO:0000305}.
-!- DOMAIN: Botulinum neurotoxin E light chain: Has protease activity
(By similarity). {ECO:0000250|UniProtKB:Q00496}.
-!- DOMAIN: Botulinum neurotoxin E heavy chain: Has 3 functional
domains; the translocation domain (TD) and the receptor-binding
domain (RBD) which is further subdivided into N- and C-terminal
domains (N-RBD and C-RBD) (By similarity). In BoNT/E the domains
are arranged differently than BoNT/A and BoNT/B; in BoNT/E the LC
and RBD are on the same side of the TD and are in contact, whereas
in BoNT/A and BoNT/B the LC is separated from the RBD by the TD
(By similarity). The putative transmembrane region is closer to
the receptor-binding regions in this toxin, which may explain why
it acts faster than BoNT/A and BoNT/B (By similarity). The N-
terminus of the TD wraps an extended belt around the perimeter of
the LC, protecting Zn(2+) in the active site and may be a
pseudosubstrate inhibitor which serves as an intramolecular
chaperone for the LC prior to its translocation into the host
cytosol (By similarity). The RBD binds transiently exposed
coreceptors on the host presynaptic cell membrane (By similarity).
{ECO:0000250|UniProtKB:Q00496}.
-!- MISCELLANEOUS: There are seven antigenically distinct forms of
botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes
are quite frequent.
-!- MISCELLANEOUS: Botulism poisoning is usually food-borne, either by
ingesting toxin or bacterial-contaminated food, or less frequently
by inhalation poisoning. In both cases the neurotoxin binds to the
apical surface of epithelial cells in the gut or airway. Toxin
undergoes receptor-mediated endocytosis (using a different
receptor than on target nerve cells), transcytosis across the
epithelial cells and release into the general circulation. Once in
the general circulation it binds to its target cells.
{ECO:0000250|UniProtKB:P0DPI0}.
-!- MISCELLANEOUS: Unlike botulinum neurotoxin type A, type E is
released from bacteria as a single chain and cleaved by host
proteases into the active dichain (Probable).
{ECO:0000250|UniProtKB:Q00496, ECO:0000305}.
-!- MISCELLANEOUS: Types A, B and E are the most frequent cause of
adult human foodborne botulism; type A is the most severe, while
type E has the shortest incubation period (By similarity). Type E
neurotoxin from C.butyricum strains ATCC 43181, ATCC 43775 and
BL6340 were all isolated from cases of human infant botulism
(PubMed:1543481, PubMed:2033376). {ECO:0000250|UniProtKB:Q00496,
ECO:0000269|PubMed:1543481, ECO:0000269|PubMed:2033376}.
-!- 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:0008320; F:protein transmembrane transporter activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0046929; P:negative regulation of neurotransmitter secretion; 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;
Direct protein sequencing; Disulfide bond; Host cell junction;
Host cell membrane; Host cytoplasm; Host cytoplasmic vesicle;
Host membrane; Host synapse; Hydrolase; Lipid-binding; Membrane;
Metal-binding; Metalloprotease; Neurotoxin; Protease; Secreted; Toxin;
Transmembrane; Virulence; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.3}.
CHAIN 2 1251 Botulinum neurotoxin type E.
/FTId=PRO_0000444920.
CHAIN 2 422 Botulinum neurotoxin E light chain.
/FTId=PRO_0000029223.
CHAIN 423 1251 Botulinum neurotoxin E heavy chain.
/FTId=PRO_0000029224.
REGION 423 819 Translocation domain (TD).
{ECO:0000250|UniProtKB:Q00496}.
REGION 466 515 Belt. {ECO:0000250|UniProtKB:Q00496}.
REGION 845 1067 N-terminus of receptor binding domain (N-
RBD). {ECO:0000250|UniProtKB:P0DPI0}.
REGION 1068 1251 C-terminus of receptor binding domain (C-
RBD). {ECO:0000250|UniProtKB:P0DPI0}.
MOTIF 1221 1224 Host ganglioside-binding motif.
{ECO:0000250|UniProtKB:P0DPI0}.
ACT_SITE 213 213 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 212 212 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 216 216 Zinc; via tele nitrogen; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 251 251 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q00496}.
DISULFID 412 426 Interchain (between light and heavy
chains). {ECO:0000250|UniProtKB:P0DPI0,
ECO:0000305}.
MUTAGEN 1093 1093 K->A,R: Wild-type binding of heavy chain
to ganglioside GD1a.
{ECO:0000269|PubMed:21849494}.
MUTAGEN 1214 1214 K->A: Loss of heavy chain binding to
ganglioside GD1a.
{ECO:0000269|PubMed:21849494}.
MUTAGEN 1214 1214 K->H: Signficant decrease in heavy chain
binding to ganglioside GD1a.
{ECO:0000269|PubMed:21849494}.
MUTAGEN 1229 1229 R->A: Wild-type binding of heavy chain to
ganglioside GD1a.
{ECO:0000269|PubMed:21849494}.
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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