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

 BXF_CLOBO               Reviewed;        1274 AA.
P30996;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
12-SEP-2018, entry version 150.
RecName: Full=Botulinum neurotoxin type F;
Short=BoNT/F {ECO:0000303|PubMed:7764998};
AltName: Full=Bontoxilysin-F;
Contains:
RecName: Full=Botulinum neurotoxin F light chain;
Short=LC;
EC=3.4.24.69 {ECO:0000269|PubMed:8505288};
Contains:
RecName: Full=Botulinum neurotoxin F heavy chain;
Short=HC;
Flags: Precursor;
Name=botF;
Clostridium botulinum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1491;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 23387 / Type F;
PubMed=1398040; DOI=10.1016/0378-1097(92)90408-G;
East A.K., Richardson P.T., Allaway D., Collins M.D., Roberts T.A.,
Thompson D.E.;
"Sequence of the gene encoding type F neurotoxin of Clostridium
botulinum.";
FEMS Microbiol. Lett. 75:225-230(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
STRAIN=Hobbs FT10 / Type F;
PubMed=7764998; DOI=10.1007/BF01575751;
East A.K., Collins M.D.;
"Conserved structure of genes encoding components of botulinum
neurotoxin complex M and the sequence of the gene coding for the
nontoxic component in nonproteolytic Clostridium botulinum type F.";
Curr. Microbiol. 29:69-77(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-1002.
STRAIN=Craig 610 / Type F, and Hobbs FT10 / Type F;
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).
[4]
FUNCTION (BOTULINUM NEUROTOXIN F LIGHT CHAIN), IDENTIFICATION OF
SUBSTRATE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, AND
SUBCELLULAR LOCATION (BOTULINUM NEUROTOXIN F LIGHT CHAIN).
STRAIN=Type F;
PubMed=8505288;
Schiavo G., Shone C.C., Rossetto O., Alexander F.C., Montecucco C.;
"Botulinum neurotoxin serotype F is a zinc endopeptidase specific for
VAMP/synaptobrevin.";
J. Biol. Chem. 268:11516-11519(1993).
[5]
IDENTIFICATION OF SUBSTRATE, AND SUBCELLULAR LOCATION (BOTULINUM
NEUROTOXIN F LIGHT CHAIN).
STRAIN=Type F;
PubMed=8175689;
Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F.,
Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H.;
"Cleavage of members of the synaptobrevin/VAMP family by types D and F
botulinal neurotoxins and tetanus toxin.";
J. Biol. Chem. 269:12764-12772(1994).
[6]
FUNCTION (BOTULINUM NEUROTOXIN F LIGHT CHAIN), AND CATALYTIC ACTIVITY.
STRAIN=Type F;
PubMed=8197120; DOI=10.1073/pnas.91.11.4688;
Yamasaki S., Hu Y., Binz T., Kalkuhl A., Kurazono H., Tamura T.,
Jahn R., Kandel E., Niemann H.;
"Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia
californica: structure and proteolysis by tetanus toxin and botulinal
neurotoxins type D and F.";
Proc. Natl. Acad. Sci. U.S.A. 91:4688-4692(1994).
[7]
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).
[8] {ECO:0000244|PDB:2A8A, ECO:0000244|PDB:2A97}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-439 IN COMPLEX WITH ZINC,
FUNCTION (BOTULINUM NEUROTOXIN F LIGHT CHAIN), AND COFACTOR.
PubMed=16128577; DOI=10.1021/bi0510072;
Agarwal R., Binz T., Swaminathan S.;
"Structural analysis of botulinum neurotoxin serotype F light chain:
implications on substrate binding and inhibitor design.";
Biochemistry 44:11758-11765(2005).
-!- FUNCTION: Botulinum neurotoxin type F: Botulinum toxin causes
flaccid paralysis by inhibiting neurotransmitter (acetylcholine)
release from the presynaptic membranes of nerve terminals of the
eukaryotic host skeletal and autonomic nervous system, with
frequent heart or respiratory failure. Precursor of botulinum
neurotoxin F which may have 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). Whole toxin only has
protease activity after reduction, which releases LC
(PubMed:8505288). Requires complex eukaryotic host
polysialogangliosides for full neurotoxicity (By similarity). It
is not clear whether a synaptic vesicle protein acts as its
receptor; there is evidence for and against SV2 fulfilling this
function (By similarity). {ECO:0000250|UniProtKB:A7GBG3,
ECO:0000269|PubMed:8505288}.
-!- FUNCTION: Botulinum neurotoxin F light chain: Has proteolytic
activity (PubMed:8505288, PubMed:8175689, PubMed:8197120). After
translocation into the eukaryotic host cytosol, inhibits
neurotransmitter release by acting as a zinc endopeptidase that
catalyzes the hydrolysis of the '60-Gln-|-Lys-61' bond of
synaptobrevin-1/VAMP1 and the equivalent 'Gln-|-Lys' sites in
VAMP2 and VAMP3 (PubMed:8505288, PubMed:8175689). Cleaves the '48-
Gln-|-Lys-49' bond of A.californica synaptobrevin (AC P35589)
(PubMed:8197120). {ECO:0000269|PubMed:8175689,
ECO:0000269|PubMed:8197120, ECO:0000269|PubMed:8505288,
ECO:0000305|PubMed:16128577}.
-!- FUNCTION: Botulinum neurotoxin F 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; polysialated gangliosides
and the receptor protein SV2A, SV2B and SV2C in close proximity on
host synaptic vesicles; although not all evidence indicates these
are the receptors (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; 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). {ECO:0000250|UniProtKB:A7GBG3}.
-!- CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the
neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No
detected action on small molecule substrates.
{ECO:0000269|PubMed:8197120, ECO:0000269|PubMed:8505288}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16128577,
ECO:0000305|PubMed:8505288};
Note=Binds 1 zinc ion per subunit (PubMed:8505288,
PubMed:16128577). {ECO:0000269|PubMed:16128577,
ECO:0000305|PubMed:8505288};
-!- ACTIVITY REGULATION: Proteolysis inhibited by 1,10-phenanthroline,
captopril and EDTA (PubMed:8505288). {ECO:0000269|PubMed:8505288}.
-!- 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, SV2B and SV2C (By similarity).
{ECO:0000250|UniProtKB:A7GBG3}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin type F: Secreted
{ECO:0000250|UniProtKB:P0DPI0}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin F light chain: Secreted
{ECO:0000250|UniProtKB:P0DPI0}. Host cytoplasm, host cytosol
{ECO:0000305|PubMed:8175689, ECO:0000305|PubMed:8505288}.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin F heavy chain: Secreted
{ECO:0000250|UniProtKB:P0DPI0}. Host cell junction, host synapse,
host presynaptic cell membrane {ECO:0000305}. Host cytoplasmic
vesicle, host secretory vesicle, host synaptic vesicle membrane
{ECO:0000250|UniProtKB:P0DPI0}; Multi-pass membrane protein
{ECO:0000305}.
-!- DOMAIN: Botulinum neurotoxin F light chain: Has protease activity
(PubMed:8505288, PubMed:8175689, PubMed:8197120).
{ECO:0000269|PubMed:8175689, ECO:0000269|PubMed:8197120,
ECO:0000269|PubMed:8505288}.
-!- DOMAIN: Botulinum neurotoxin F 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). 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:A7GBG3}.
-!- 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}.
-!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
-!- CAUTION: It is not clear whether a synaptic vesicle protein acts
as its receptor; there is evidence for and against SV2 fulfilling
this function. {ECO:0000305}.
-!- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial
Neurotoxins;
URL="https://botdb.abcc.ncifcrf.gov/";
-----------------------------------------------------------------------
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EMBL; M92906; AAA23263.1; -; Genomic_DNA.
EMBL; S73676; AAC60475.1; -; Genomic_DNA.
EMBL; X70820; CAA50151.1; -; Genomic_DNA.
EMBL; X70816; CAA50147.1; -; Genomic_DNA.
PIR; I40813; I40813.
PIR; S48109; S48109.
PDB; 2A8A; X-ray; 2.00 A; A=1-439.
PDB; 2A97; X-ray; 1.80 A; A/B=1-439.
PDBsum; 2A8A; -.
PDBsum; 2A97; -.
ProteinModelPortal; P30996; -.
SMR; P30996; -.
IntAct; P30996; 2.
MINT; P30996; -.
BindingDB; P30996; -.
ChEMBL; CHEMBL2007627; -.
MEROPS; M27.002; -.
BRENDA; 3.4.24.69; 1462.
Reactome; R-HSA-5250981; Toxicity of botulinum toxin type F (BoNT/F).
EvolutionaryTrace; P30996; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044161; C:host cell cytoplasmic vesicle; 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:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome.
GO; GO:0008320; F:protein transmembrane transporter activity; TAS:Reactome.
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;
3D-structure; 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.
CHAIN 1 1274 Botulinum neurotoxin type F.
/FTId=PRO_0000444921.
CHAIN 1 436 Botulinum neurotoxin F light chain.
/FTId=PRO_0000029225.
CHAIN 437 1274 Botulinum neurotoxin F heavy chain.
/FTId=PRO_0000029226.
REGION 440 862 Translocation domain (TD).
{ECO:0000250|UniProtKB:P0DPI0}.
REGION 485 534 Belt. {ECO:0000250|UniProtKB:P0DPI0}.
REGION 863 1087 N-terminus of receptor binding domain (N-
RBD). {ECO:0000250|UniProtKB:P0DPI0}.
REGION 1088 1274 C-terminus of receptor binding domain (C-
RBD). {ECO:0000250|UniProtKB:P0DPI0}.
MOTIF 1245 1248 Host ganglioside-binding motif.
{ECO:0000250|UniProtKB:P0DPI0}.
ACT_SITE 228 228 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 227 227 Zinc; via tele nitrogen; catalytic.
{ECO:0000244|PDB:2A8A,
ECO:0000244|PDB:2A97,
ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:16128577}.
METAL 231 231 Zinc; via tele nitrogen; catalytic.
{ECO:0000244|PDB:2A8A,
ECO:0000244|PDB:2A97,
ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:16128577}.
METAL 266 266 Zinc; catalytic. {ECO:0000244|PDB:2A8A,
ECO:0000244|PDB:2A97,
ECO:0000269|PubMed:16128577}.
DISULFID 429 445 Interchain (between light and heavy
chains). {ECO:0000250|UniProtKB:P0DPI0,
ECO:0000305}.
STRAND 16 22 {ECO:0000244|PDB:2A97}.
HELIX 28 30 {ECO:0000244|PDB:2A97}.
STRAND 34 40 {ECO:0000244|PDB:2A97}.
STRAND 43 49 {ECO:0000244|PDB:2A97}.
HELIX 56 59 {ECO:0000244|PDB:2A97}.
STRAND 69 71 {ECO:0000244|PDB:2A97}.
TURN 75 78 {ECO:0000244|PDB:2A97}.
HELIX 81 98 {ECO:0000244|PDB:2A97}.
HELIX 102 113 {ECO:0000244|PDB:2A97}.
TURN 133 135 {ECO:0000244|PDB:2A97}.
STRAND 136 140 {ECO:0000244|PDB:2A97}.
STRAND 146 150 {ECO:0000244|PDB:2A97}.
STRAND 152 157 {ECO:0000244|PDB:2A97}.
STRAND 166 169 {ECO:0000244|PDB:2A97}.
HELIX 182 184 {ECO:0000244|PDB:2A97}.
STRAND 185 187 {ECO:0000244|PDB:2A97}.
STRAND 191 194 {ECO:0000244|PDB:2A97}.
STRAND 199 203 {ECO:0000244|PDB:2A97}.
STRAND 216 218 {ECO:0000244|PDB:2A8A}.
HELIX 221 236 {ECO:0000244|PDB:2A97}.
TURN 241 245 {ECO:0000244|PDB:2A97}.
STRAND 247 251 {ECO:0000244|PDB:2A8A}.
TURN 253 256 {ECO:0000244|PDB:2A8A}.
STRAND 259 263 {ECO:0000244|PDB:2A8A}.
HELIX 264 270 {ECO:0000244|PDB:2A97}.
HELIX 272 277 {ECO:0000244|PDB:2A97}.
HELIX 280 303 {ECO:0000244|PDB:2A97}.
HELIX 313 323 {ECO:0000244|PDB:2A97}.
STRAND 326 328 {ECO:0000244|PDB:2A97}.
STRAND 334 336 {ECO:0000244|PDB:2A97}.
HELIX 338 348 {ECO:0000244|PDB:2A97}.
HELIX 353 360 {ECO:0000244|PDB:2A97}.
STRAND 366 369 {ECO:0000244|PDB:2A97}.
STRAND 374 376 {ECO:0000244|PDB:2A97}.
TURN 383 385 {ECO:0000244|PDB:2A97}.
TURN 388 390 {ECO:0000244|PDB:2A97}.
HELIX 395 404 {ECO:0000244|PDB:2A97}.
TURN 406 408 {ECO:0000244|PDB:2A97}.
HELIX 410 412 {ECO:0000244|PDB:2A97}.
SEQUENCE 1274 AA; 146710 MW; 5B99756A7438B921 CRC64;
MPVAINSFNY NDPVNDDTIL YMQIPYEEKS KKYYKAFEIM RNVWIIPERN TIGTNPSDFD
PPASLKNGSS AYYDPNYLTT DAEKDRYLKT TIKLFKRINS NPAGKVLLQE ISYAKPYLGN
DHTPIDEFSP VTRTTSVNIK LSTNVESSML LNLLVLGAGP DIFESCCYPV RKLIDPDVVY
DPSNYGFGSI NIVTFSPEYE YTFNDISGGH NSSTESFIAD PAISLAHELI HALHGLYGAR
GVTYEETIEV KQAPLMIAEK PIRLEEFLTF GGQDLNIITS AMKEKIYNNL LANYEKIATR
LSEVNSAPPE YDINEYKDYF QWKYGLDKNA DGSYTVNENK FNEIYKKLYS FTESDLANKF
KVKCRNTYFI KYEFLKVPNL LDDDIYTVSE GFNIGNLAVN NRGQSIKLNP KIIDSIPDKG
LVEKIVKFCK SVIPRKGTKA PPRLCIRVNN SELFFVASES SYNENDINTP KEIDDTTNLN
NNYRNNLDEV ILDYNSQTIP QISNRTLNTL VQDNSYVPRY DSNGTSEIEE YDVVDFNVFF
YLHAQKVPEG ETNISLTSSI DTALLEESKD IFFSSEFIDT INKPVNAALF IDWISKVIRD
FTTEATQKST VDKIADISLI VPYVGLALNI IIEAEKGNFE EAFELLGVGI LLEFVPELTI
PVILVFTIKS YIDSYENKNK AIKAINNSLI EREAKWKEIY SWIVSNWLTR INTQFNKRKE
QMYQALQNQV DAIKTAIEYK YNNYTSDEKN RLESEYNINN IEEELNKKVS LAMKNIERFM
TESSISYLMK LINEAKVGKL KKYDNHVKSD LLNYILDHRS ILGEQTNELS DLVTSTLNSS
IPFELSSYTN DKILIIYFNR LYKKIKDSSI LDMRYENNKF IDISGYGSNI SINGNVYIYS
TNRNQFGIYN SRLSEVNIAQ NNDIIYNSRY QNFSISFWVR IPKHYKPMNH NREYTIINCM
GNNNSGWKIS LRTVRDCEII WTLQDTSGNK ENLIFRYEEL NRISNYINKW IFVTITNNRL
GNSRIYINGN LIVEKSISNL GDIHVSDNIL FKIVGCDDET YVGIRYFKVF NTELDKTEIE
TLYSNEPDPS ILKNYWGNYL LYNKKYYLFN LLRKDKYITL NSGILNINQQ RGVTEGSVFL
NYKLYEGVEV IIRKNGPIDI SNTDNFVRKN DLAYINVVDR GVEYRLYADT KSEKEKIIRT
SNLNDSLGQI IVMDSIGNNC TMNFQNNNGS NIGLLGFHSN NLVASSWYYN NIRRNTSSNG
CFWSSISKEN GWKE


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