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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.
20-JUN-2018, entry version 148.
RecName: Full=Botulinum neurotoxin type F;
Short=BoNT/F;
EC=3.4.24.69;
AltName: Full=Bontoxilysin-F;
Contains:
RecName: Full=Botulinum neurotoxin F light chain;
Contains:
RecName: Full=Botulinum neurotoxin F heavy chain;
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.
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]
IDENTIFICATION OF SUBSTRATE.
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).
-!- 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 '58-Gln-|-Lys-
59' bond of synaptobrevins-1 and -2.
-!- 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 F light chain:
Secreted. Host cytoplasm, host cytosol.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin F 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; 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.
PDB; 3FIE; X-ray; 2.10 A; A/B=5-419.
PDB; 3FII; X-ray; 2.17 A; A=5-419.
PDBsum; 2A8A; -.
PDBsum; 2A97; -.
PDBsum; 3FIE; -.
PDBsum; 3FII; -.
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: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; 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; Cleavage on pair of basic residues; 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.
CHAIN 1 436 Botulinum neurotoxin F light chain.
/FTId=PRO_0000029225.
CHAIN 437 1274 Botulinum neurotoxin F heavy chain.
/FTId=PRO_0000029226.
ACT_SITE 228 228 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 227 227 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 231 231 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
DISULFID 429 445 Interchain (between light and heavy
chains). {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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