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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.
18-JUL-2018, entry version 160.
RecName: Full=Botulinum neurotoxin type E;
Short=BoNT/E {ECO:0000303|PubMed:8408542};
AltName: Full=Bontoxilysin-E;
Contains:
RecName: Full=Botulinum neurotoxin E light chain;
Short=LC;
EC=3.4.24.69 {ECO:0000269|PubMed:8243676};
Contains:
RecName: Full=Botulinum neurotoxin E heavy chain;
Short=HC;
Flags: Precursor;
Name=botE {ECO:0000303|PubMed:1541280};
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].
STRAIN=NCTC 11219 / Type E;
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.
STRAIN=Beluga / Type E;
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.
STRAIN=Alaska E43 / Type E3;
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.
STRAIN=Alaska E43 / Type E3;
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 / ATCC 9564 / 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]
RELEASED AS SINGLE CHAIN.
STRAIN=Type E;
PubMed=6353669;
DasGupta B.R., Rasmussen S.;
"Purification and amino acid composition of type E botulinum
neurotoxin.";
Toxicon 21:535-545(1983).
[8]
RELEASED AS SINGLE CHAIN.
STRAIN=Alaska E43 / Type E3;
PubMed=4030755;
Sathyamoorthy V., DasGupta B.R.;
"Separation, purification, partial characterization and comparison of
the heavy and light chains of botulinum neurotoxin types A, B, and
E.";
J. Biol. Chem. 260:10461-10466(1985).
[9]
IDENTIFICATION AS A ZINC-BINDING PROTEIN, AND COFACTOR.
STRAIN=Type E;
PubMed=1429690;
Schiavo G., Rossetto O., Santucci A., Dasgupta B.R., Montecucco C.;
"Botulinum neurotoxins are zinc proteins.";
J. Biol. Chem. 267:23479-23483(1992).
[10]
HOST RANGE, AND EPIDEMIOLOGY.
PubMed=1431246;
Woodruff B.A., Griffin P.M., McCroskey L.M., Smart J.F.,
Wainwright R.B., Bryant R.G., Hutwagner L.C., Hatheway C.L.;
"Clinical and laboratory comparison of botulism from toxin types A, B,
and E in the United States, 1975-1988.";
J. Infect. Dis. 166:1281-1286(1992).
[11]
FUNCTION (BOTULINUM NEUROTOXIN E LIGHT CHAIN), IDENTIFICATION OF
SUBSTRATE, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION (BOTULINUM
NEUROTOXIN E LIGHT CHAIN).
STRAIN=Type E;
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).
[12]
FUNCTION (BOTULINUM NEUROTOXIN TYPE E AND BOTULINUM NEUROTOXIN E LIGHT
CHAIN), IDENTIFICATION OF SUBSTRATE, CATALYTIC ACTIVITY, ENZYME
REGULATION, AND SUBCELLULAR LOCATION (BOTULINUM NEUROTOXIN E LIGHT
CHAIN).
STRAIN=Beluga / Type E;
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).
[13]
FUNCTION (BOTULINUM NEUROTOXIN E HEAVY CHAIN), AND SUBCELLULAR
LOCATION (BOTULINUM NEUROTOXIN E HEAVY CHAIN).
STRAIN=NCTC 11219 / Type E;
PubMed=10413679;
Lalli G., Herreros J., Osborne S.L., Montecucco C., Rossetto O.,
Schiavo G.;
"Functional characterisation of tetanus and botulinum neurotoxins
binding domains.";
J. Cell Sci. 112:2715-2724(1999).
[14]
FUNCTION (BOTULINUM NEUROTOXIN E LIGHT CHAIN), SUBSTRATE SPECIFICITY,
AND CATALYTIC ACTIVITY.
STRAIN=Beluga / Type E;
PubMed=9886085;
Vaidyanathan V.V., Yoshino K., Jahnz M., Doerries C., Bade S.,
Nauenburg S., Niemann H., Binz T.;
"Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C,
and E: domains and amino acid residues controlling the formation of
enzyme-substrate complexes and cleavage.";
J. Neurochem. 72:327-337(1999).
[15]
FUNCTION (BOTULINUM NEUROTOXIN E LIGHT AND BOTULINUM NEUROTOXIN E
HEAVY CHAIN), AND DISULFIDE BOND.
STRAIN=Type E;
PubMed=17666397; DOI=10.1074/jbc.M703619200;
Fischer A., Montal M.;
"Crucial role of the disulfide bridge between botulinum neurotoxin
light and heavy chains in protease translocation across membranes.";
J. Biol. Chem. 282:29604-29611(2007).
[16]
DISCUSSION OF BELT FUNCTION, AND DOMAIN.
PubMed=17907800; DOI=10.1371/journal.ppat.0030113;
Brunger A.T., Breidenbach M.A., Jin R., Fischer A., Santos J.S.,
Montal M.;
"Botulinum neurotoxin heavy chain belt as an intramolecular chaperone
for the light chain.";
PLoS Pathog. 3:1191-1194(2007).
[17]
FUNCTION (BOTULINUM NEUROTOXIN TYPE E), IDENTIFICATION OF HOST
RECEPTOR, AND INTERACTION WITH HOST SV2A AND SV2B.
STRAIN=Type E;
PubMed=18815274; DOI=10.1091/mbc.E08-07-0765;
Dong M., Liu H., Tepp W.H., Johnson E.A., Janz R., Chapman E.R.;
"Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin
E into neurons.";
Mol. Biol. Cell 19:5226-5237(2008).
[18]
FUNCTION (BOTULINUM NEUROTOXIN E HEAVY CHAIN), AND INTERACTION WITH
HOST SV2 AND SYT1.
PubMed=19476346; DOI=10.1021/bi9002138;
Fu Z., Chen C., Barbieri J.T., Kim J.J., Baldwin M.R.;
"Glycosylated SV2 and gangliosides as dual receptors for botulinum
neurotoxin serotype F.";
Biochemistry 48:5631-5641(2009).
[19]
FUNCTION (BOTULINUM NEUROTOXIN TYPE E AND BOTULINUM NEUROTOXIN E HEAVY
CHAIN), INTERACTION WITH HOST SV2A AND SV2B, GANGLIOSIDE-BINDING, AND
MUTAGENESIS OF GLU-1172 AND TRP-1223.
STRAIN=NCTC 11219 / Type E;
PubMed=19650874; DOI=10.1111/j.1471-4159.2009.06298.x;
Rummel A., Haefner K., Mahrhold S., Darashchonak N., Holt M., Jahn R.,
Beermann S., Karnath T., Bigalke H., Binz T.;
"Botulinum neurotoxins C, E and F bind gangliosides via a conserved
binding site prior to stimulation-dependent uptake with botulinum
neurotoxin F utilising the three isoforms of SV2 as second receptor.";
J. Neurochem. 110:1942-1954(2009).
[20]
FUNCTION (BOTULINUM NEUROTOXIN TYPE E), SUBUNIT, AND SUBCELLULAR
LOCATION (BOTULINUM NEUROTOXIN TYPE E).
STRAIN=Type E;
PubMed=22720883; DOI=10.1021/bi3004928;
Sun S., Tepp W.H., Johnson E.A., Chapman E.R.;
"Botulinum neurotoxins B and E translocate at different rates and
exhibit divergent responses to GT1b and low pH.";
Biochemistry 51:5655-5662(2012).
[21]
REVIEW.
PubMed=28356439; DOI=10.1124/pr.116.012658;
Pirazzini M., Rossetto O., Eleopra R., Montecucco C.;
"Botulinum neurotoxins: Biology, pharmacology, and toxicology.";
Pharmacol. Rev. 69:200-235(2017).
[22] {ECO:0000244|PDB:1T3A, ECO:0000244|PDB:1T3C}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-422 IN COMPLEX WITH ZINC,
FUNCTION (BOTULINUM NEUROTOXIN E LIGHT CHAIN), REACTION MECHANISM,
ACTIVE SITE, COFACTOR, AND MUTAGENESIS OF GLU-213.
STRAIN=Type E;
PubMed=15157097; DOI=10.1021/bi036278w;
Agarwal R., Eswaramoorthy S., Kumaran D., Binz T., Swaminathan S.;
"Structural analysis of botulinum neurotoxin type E catalytic domain
and its mutant Glu212-->Gln reveals the pivotal role of the Glu212
carboxylate in the catalytic pathway.";
Biochemistry 43:6637-6644(2004).
[23] {ECO:0000244|PDB:1ZKW, ECO:0000244|PDB:1ZKX, ECO:0000244|PDB:1ZL5, ECO:0000244|PDB:1ZL6, ECO:0000244|PDB:1ZN3}
X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF MUTATED 2-421 IN COMPLEX
WITH ZINC, FUNCTION (BOTULINUM NEUROTOXIN E LIGHT CHAIN), REACTION
MECHANISM, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, AND
MUTAGENESIS OF 159-GLU--ASN-161; GLU-250; GLU-336; ARG-348 AND
TYR-351.
STRAIN=Type E;
PubMed=15938619; DOI=10.1021/bi050253a;
Agarwal R., Binz T., Swaminathan S.;
"Analysis of active site residues of botulinum neurotoxin E by
mutational, functional, and structural studies: Glu335Gln is an
apoenzyme.";
Biochemistry 44:8291-8302(2005).
[24]
STRUCTURE BY ELECTRON MICROSCOPY (24.0 ANGSTROMS), AND DOMAIN.
STRAIN=Type E;
PubMed=18032388; DOI=10.1074/jbc.M707917200;
Fischer A., Garcia-Rodriguez C., Geren I., Lou J., Marks J.D.,
Nakagawa T., Montal M.;
"Molecular architecture of botulinum neurotoxin E revealed by single
particle electron microscopy.";
J. Biol. Chem. 283:3997-4003(2008).
[25] {ECO:0000244|PDB:3FFZ}
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR,
DOMAIN, AND DISULFIDE BONDS.
STRAIN=Type E;
PubMed=19118561; DOI=10.1016/j.jmb.2008.12.027;
Kumaran D., Eswaramoorthy S., Furey W., Navaza J., Sax M.,
Swaminathan S.;
"Domain organization in Clostridium botulinum neurotoxin type E is
unique: its implication in faster translocation.";
J. Mol. Biol. 386:233-245(2009).
-!- 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 (PubMed:19476346,
PubMed:19650874). 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 (PubMed:22720883). 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). Electrical stimulation
increases uptake of toxin, probably by transiently exposing a
receptor found in eukaryotic target synaptic vesicles
(PubMed:19476346, PubMed:19650874). Uses the large lumenal domain
of synaptic vesicle glycoproteins 2A and 2B (SV2A and SV2B) but
not SV2C as receptor; an N-linked glycan of SV2 is essential for
receptor function (PubMed:18815274, PubMed:19476346). Host cell
gangliosides are also required for neurotoxin uptake and full
toxicity (PubMed:18815274, PubMed:19650874). BoNT/E is a
'coincidence detector'; it requires simultaneous binding to
coreceptor GT1b and low pH to transform into a membrane-bound,
oligomeric channel (PubMed:22720883). Requires trypsinization and
reduction before it can be used in assays in vitro
(PubMed:8294407). {ECO:0000250|UniProtKB:P0DPI0,
ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:19476346,
ECO:0000269|PubMed:19650874, ECO:0000269|PubMed:22720883,
ECO:0000305|PubMed:8294407}.
-!- FUNCTION: Botulinum neurotoxin E light chain: Has proteolytic
activity (PubMed:8243676, PubMed:8294407, PubMed:9886085). After
translocation into the eukaryotic host cytosol, inhibits
neurotransmitter release by acting as a zinc endopeptidase that
catalyzes the hydrolysis of the '180-Arg-|-Ile-181' bond in SNAP25
(PubMed:8243676, PubMed:8294407, PubMed:9886085). Hydrolyzes the
'185-Arg-|-Ile-186' bond of mouse SNAP23, but not in human which
has a different sequence (PubMed:9886085). Recognizes the '146-
Met--Asp-186' region of SNAP25 (PubMed:9886085). The reaction
mechanism probably has a nucleophilic water held in place by Glu-
213 (PubMed:15157097, PubMed:15938619). Reduction of the
interchain disulfide bond occurs in the host cytosol and probably
prevents retrotranslocation into the synaptic vesicle
(PubMed:17666397). {ECO:0000269|PubMed:15157097,
ECO:0000269|PubMed:15938619, ECO:0000269|PubMed:17666397,
ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407,
ECO:0000269|PubMed:9886085}.
-!- 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
(PubMed:17666397). 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 (PubMed:10413679). It probably
simultaneously recognizes 2 coreceptors; polysialated gangliosides
and either of the receptor proteins SV2A and SV2B in close
proximity on host synaptic vesicles (PubMed:18815274,
PubMed:19650874, PubMed:19476346). The N-terminus of the TD wraps
an extended belt around the perimeter of the light chain (LC),
protecting Zn(2+) in the active site (PubMed:19118561). The belt
may also prevent premature LC dissociation from the translocation
channel and protect toxin prior to translocation
(PubMed:17907800). The TD inserts into synaptic vesicle membrane
to allow translocation into the host cytosol (By similarity).
Responsible for adherence of the toxin to the cell surface; HC
alone prevents uptake of whole toxin by neural cells, and delays
paralysis onset by 154% (PubMed:10413679). Significantly decreases
uptake and toxicity of whole BoNT/E, but also interferes with
uptake of BoNT/C; binds GT1b in vitro (PubMed:19650874). Binds to
synaptic vesicle glycoproteins SV2A and SV2B which serve as
coreceptors with gangliosides (PubMed:18815274, PubMed:19650874).
Interaction with SV2 proteins requires SV2 glycosylation
(PubMed:19476346). HC alone significantly decreases uptake and
toxicity of whole BoNT/E (PubMed:19650874). HC is responsible for
translocation of LC into the host cytosol; an intact disulfide
bond between the 2 subunits is required for translocation, which
is reduced upon contact with the host cytosol (PubMed:17666397).
{ECO:0000250|UniProtKB:P0DPI0, ECO:0000269|PubMed:10413679,
ECO:0000269|PubMed:17666397, ECO:0000269|PubMed:18815274,
ECO:0000269|PubMed:19476346, ECO:0000269|PubMed:19650874,
ECO:0000305|PubMed:17907800}.
-!- CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the
neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No
detected action on small molecule substrates.
{ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407,
ECO:0000269|PubMed:9886085}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:1429690,
ECO:0000269|PubMed:15157097, ECO:0000269|PubMed:15938619,
ECO:0000269|PubMed:19118561};
Note=Binds 1 zinc ion per subunit (PubMed:1429690,
PubMed:15157097, PubMed:15938619, PubMed:19118561).
{ECO:0000269|PubMed:1429690, ECO:0000269|PubMed:15157097,
ECO:0000269|PubMed:15938619, ECO:0000269|PubMed:19118561};
-!- ENZYME REGULATION: Proteolysis of SNAP25 by whole toxin inhibited
by dipicolinic acid, 1,10-phenanthroline and EDTA
(PubMed:8294407). {ECO:0000269|PubMed:8294407}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.9 uM for purified SNAP25 with botulinum neurotoxin E light
chain {ECO:0000269|PubMed:15938619};
Note=kcat is 257 min (-1) with botulinum neurotoxin E light
chain. {ECO:0000269|PubMed:15938619};
-!- SUBUNIT: Heterodimer; disulfide-linked heterodimer of a light
chain (LC) and a heavy chain (HC); cleavage occurs after bacterial
export by host proteases (PubMed:6353669, PubMed:4030755,
PubMed:19118561). The LC has the proteolytic/pharmacological
activity, while the N- and C-terminal of the HC mediate channel
formation and toxin binding, respectively. Oligomerizes in the
presence of coreceptor ganglioside GT1b between pH 4.4 and 8.0; it
might oligomerize on host cell surface (PubMed:22720883).
Interacts with host synaptic vesicle glycoproteins SV2A and SV2B
(PubMed:18815274, PubMed:19650874). HC interacts with a complex
including at least host SV2 and synaptotagmin-1 (SYT1);
copurification depends on glycosylation of SV2 (PubMed:19476346).
{ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:19118561,
ECO:0000269|PubMed:19476346, ECO:0000269|PubMed:19650874,
ECO:0000269|PubMed:22720883, ECO:0000269|PubMed:4030755,
ECO:0000269|PubMed:6353669}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin type E: Secreted
{ECO:0000305|PubMed:8294407}. Note=At pH 4.4 in the presence of
ganglioside GT1b, becomes a membrane-associated hydrophobic
protein (PubMed:22720883). {ECO:0000269|PubMed:22720883}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin E light chain:
Secreted. Host cytoplasm, host cytosol
{ECO:0000305|PubMed:8243676, ECO:0000305|PubMed:8294407}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin E heavy chain:
Secreted. Host cell junction, host synapse, host presynaptic cell
membrane {ECO:0000305|PubMed:10413679}. 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
(PubMed:8243676, PubMed:8294407, PubMed:9886085).
{ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407,
ECO:0000269|PubMed:9886085}.
-!- 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) (PubMed:19118561). 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
(PubMed:19118561). 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 (PubMed:19118561). The N-
terminus of the TD wraps an extended belt around the perimeter of
the LC, partially protecting Zn(2+) in the active site
(PubMed:19118561). The belt may be a pseudosubstrate inhibitor
which serves as an intramolecular chaperone for the LC prior to
its translocation into the host cytosol (PubMed:17907800). The RBD
binds transiently exposed coreceptors on the host presynaptic cell
membrane (PubMed:18815274, PubMed:19650874, PubMed:19476346).
{ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:19118561,
ECO:0000269|PubMed:19476346, ECO:0000269|PubMed:19650874,
ECO:0000305|PubMed:17907800}.
-!- BIOTECHNOLOGY: Double mutants Gln-213/Gln-336 or Gln-213/Ala-351
might be suitable as vaccine candiates (PubMed:15938619).
{ECO:0000305|PubMed:15938619}.
-!- 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: 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 (PubMed:1431246).
{ECO:0000269|PubMed:1431246}.
-!- 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 (PubMed:6353669, PubMed:4030755,
PubMed:19118561, PubMed:8294407). {ECO:0000269|PubMed:19118561,
ECO:0000269|PubMed:4030755, ECO:0000269|PubMed:6353669,
ECO:0000305|PubMed:8294407}.
-!- 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; 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: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;
3D-structure; 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|PubMed:3888113}.
CHAIN 2 1251 Botulinum neurotoxin type E.
/FTId=PRO_0000444907.
CHAIN 2 422 Botulinum neurotoxin E light chain.
/FTId=PRO_0000029221.
CHAIN 423 1251 Botulinum neurotoxin E heavy chain.
/FTId=PRO_0000029222.
REGION 423 819 Translocation domain (TD).
{ECO:0000305|PubMed:19118561}.
REGION 466 515 Belt. {ECO:0000305|PubMed:19118561}.
REGION 845 1067 N-terminus of receptor binding domain (N-
RBD). {ECO:0000305|PubMed:19118561}.
REGION 850 1251 Receptor-binding domain (TD).
{ECO:0000305|PubMed:19118561}.
REGION 1068 1251 C-terminus of receptor binding domain (C-
RBD). {ECO:0000305|PubMed:19118561}.
MOTIF 1221 1224 Host ganglioside-binding motif.
{ECO:0000250|UniProtKB:P0DPI0,
ECO:0000305|PubMed:19650874}.
ACT_SITE 213 213 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10095,
ECO:0000305|PubMed:15157097}.
METAL 212 212 Zinc; via tele nitrogen; catalytic.
{ECO:0000244|PDB:1T3A,
ECO:0000244|PDB:1T3C,
ECO:0000244|PDB:1ZKW,
ECO:0000244|PDB:1ZKX,
ECO:0000244|PDB:1ZL6,
ECO:0000244|PDB:1ZN3,
ECO:0000244|PDB:3FFZ,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 216 216 Zinc; via tele nitrogen; catalytic.
{ECO:0000244|PDB:1T3A,
ECO:0000244|PDB:1T3C,
ECO:0000244|PDB:1ZKW,
ECO:0000244|PDB:1ZKX,
ECO:0000244|PDB:1ZL6,
ECO:0000244|PDB:1ZN3,
ECO:0000244|PDB:3FFZ,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 251 251 Zinc; catalytic. {ECO:0000244|PDB:1T3A,
ECO:0000244|PDB:1T3C,
ECO:0000244|PDB:1ZKW,
ECO:0000244|PDB:1ZKX,
ECO:0000244|PDB:1ZL6,
ECO:0000244|PDB:1ZN3,
ECO:0000244|PDB:3FFZ}.
DISULFID 412 426 Interchain (between light and heavy
chains). {ECO:0000244|PDB:3FFZ,
ECO:0000269|PubMed:19118561,
ECO:0000305|PubMed:17666397}.
MUTAGEN 159 161 ETN->AAA: KM for SNAP25 unchanged, kcat
10-fold reduced.
{ECO:0000269|PubMed:15938619}.
MUTAGEN 213 213 E->Q: No cleavage of SNAP25.
{ECO:0000269|PubMed:15157097}.
MUTAGEN 250 250 E->A: KM unchanged, kcat 10-fold reduced.
{ECO:0000269|PubMed:15938619}.
MUTAGEN 336 336 E->A: KM unchanged, kcat 30-fold reduced,
binds zinc in crystal.
{ECO:0000269|PubMed:15938619}.
MUTAGEN 336 336 E->Q: No cleavage of SNAP25. KM
unchanged, kcat 5700-fold reduced, zinc
replaced by H(2)O in crystal.
{ECO:0000269|PubMed:15157097,
ECO:0000269|PubMed:15938619}.
MUTAGEN 348 348 R->A: KM unchanged, kcat 700-fold
reduced. {ECO:0000269|PubMed:15938619}.
MUTAGEN 351 351 Y->A: No cleavage of SNAP25.
{ECO:0000269|PubMed:15938619}.
MUTAGEN 1172 1172 E->A: Significantly decreased toxicity,
dramatically decreased binding of heavy
chain to synaptosomes, significantly
decreased binding to ganglioside GT1b.
{ECO:0000269|PubMed:19650874}.
MUTAGEN 1223 1223 W->L: Dramatically decreased toxicity,
dramatically decreased binding of heavy
chain to synaptosomes, dramatically
decreased binding to ganglioside GT1b.
{ECO:0000269|PubMed:19650874}.
CONFLICT 177 177 R -> G (in Ref. 2; CAA44558).
{ECO:0000305}.
CONFLICT 198 198 C -> S (in Ref. 2; CAA44558 and 3; no
nucleotide entry). {ECO:0000305}.
CONFLICT 340 340 R -> A (in Ref. 2; CAA44558).
{ECO:0000305}.
CONFLICT 773 773 I -> L (in Ref. 2; CAA44558 and 6;
CAA50146). {ECO:0000305}.
CONFLICT 963 964 FE -> LQ (in Ref. 2; CAA44558 and 6;
CAA50146). {ECO:0000305}.
CONFLICT 967 967 R -> A (in Ref. 2; CAA44558 and 6;
CAA50146). {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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