Reviewed, UniProtKB/Swiss-Prot P30996 (BXF_CLOBO)

Names and origin

Protein names

Recommended name:
    Botulinum neurotoxin type F
      Short name=BoNT/F
    EC=3.4.24.69
Alternative name(s):
    Bontoxilysin-F
Cleaved into the following 2 chains:
    1- Recommended name:
            Botulinum neurotoxin F light chain
    2- Recommended name:
            Botulinum neurotoxin F heavy chain

Gene names

Name:

botF

Organism

Clostridium botulinum

Taxonomic identifier

1491 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	1274 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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	Binds 1 zinc ion per subunit By similarity.
Subunit structure	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. Botulinum neurotoxin F heavy chain: Secreted. Host cell junction › host synapse › host presynaptic cell membrane Potential.
Miscellaneous	There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
Sequence similarities	Belongs to the peptidase M27 family.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Membrane Secreted Synapse
Domain	Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Neurotoxin Protease Toxin
PTM	Cleavage on pair of basic residues Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	inhibition of neurotransmitter uptake Inferred from electronic annotation. Source: InterPro pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytosol Inferred from Experiment. Source: Reactome endocytic vesicle membrane Inferred from Experiment. Source: Reactome host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW synapse Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro toxin receptor binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 436

436

Botulinum neurotoxin F light chain

PRO_0000029225

Chain

437 – 1274

838

Botulinum neurotoxin F heavy chain

PRO_0000029226

Sites

Active site

228

1

By similarity

Metal binding

227

1

Zinc; catalytic By similarity

Metal binding

231

1

Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond

429 ↔ 445

Interchain (between light and heavy chains) Probable

Secondary structure

1

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1274

Helix Strand Turn

Details...

Beta strand

16 – 22

7

Helix

28 – 30

3

Beta strand

34 – 40

7

Beta strand

43 – 49

7

Helix

56 – 59

4

Turn

75 – 78

4

Helix

81 – 98

18

Helix

102 – 113

12

Turn

133 – 135

3

Beta strand

136 – 140

5

Beta strand

146 – 150

5

Beta strand

152 – 157

6

Beta strand

166 – 169

4

Turn

182 – 186

5

Beta strand

191 – 194

4

Beta strand

199 – 204

6

Beta strand

216 – 218

3

Helix

221 – 236

16

Turn

241 – 245

5

Beta strand

247 – 251

5

Turn

253 – 256

4

Beta strand

259 – 263

5

Helix

264 – 270

7

Helix

272 – 277

6

Helix

280 – 301

22

Helix

313 – 323

11

Helix

338 – 348

11

Helix

353 – 359

7

Beta strand

366 – 369

4

Beta strand

373 – 376

4

Turn

383 – 385

3

Turn

388 – 390

3

Helix

395 – 404

10

Turn

406 – 408

3

Sequences

	Sequence		Length	Mass (Da)
	P30996-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 5B99756A7438B921	FASTA	1,274	146,710
	10 20 30 40 50 60 MPVAINSFNY NDPVNDDTIL YMQIPYEEKS KKYYKAFEIM RNVWIIPERN TIGTNPSDFD 70 80 90 100 110 120 PPASLKNGSS AYYDPNYLTT DAEKDRYLKT TIKLFKRINS NPAGKVLLQE ISYAKPYLGN 130 140 150 160 170 180 DHTPIDEFSP VTRTTSVNIK LSTNVESSML LNLLVLGAGP DIFESCCYPV RKLIDPDVVY 190 200 210 220 230 240 DPSNYGFGSI NIVTFSPEYE YTFNDISGGH NSSTESFIAD PAISLAHELI HALHGLYGAR 250 260 270 280 290 300 GVTYEETIEV KQAPLMIAEK PIRLEEFLTF GGQDLNIITS AMKEKIYNNL LANYEKIATR 310 320 330 340 350 360 LSEVNSAPPE YDINEYKDYF QWKYGLDKNA DGSYTVNENK FNEIYKKLYS FTESDLANKF 370 380 390 400 410 420 KVKCRNTYFI KYEFLKVPNL LDDDIYTVSE GFNIGNLAVN NRGQSIKLNP KIIDSIPDKG 430 440 450 460 470 480 LVEKIVKFCK SVIPRKGTKA PPRLCIRVNN SELFFVASES SYNENDINTP KEIDDTTNLN 490 500 510 520 530 540 NNYRNNLDEV ILDYNSQTIP QISNRTLNTL VQDNSYVPRY DSNGTSEIEE YDVVDFNVFF 550 560 570 580 590 600 YLHAQKVPEG ETNISLTSSI DTALLEESKD IFFSSEFIDT INKPVNAALF IDWISKVIRD 610 620 630 640 650 660 FTTEATQKST VDKIADISLI VPYVGLALNI IIEAEKGNFE EAFELLGVGI LLEFVPELTI 670 680 690 700 710 720 PVILVFTIKS YIDSYENKNK AIKAINNSLI EREAKWKEIY SWIVSNWLTR INTQFNKRKE 730 740 750 760 770 780 QMYQALQNQV DAIKTAIEYK YNNYTSDEKN RLESEYNINN IEEELNKKVS LAMKNIERFM 790 800 810 820 830 840 TESSISYLMK LINEAKVGKL KKYDNHVKSD LLNYILDHRS ILGEQTNELS DLVTSTLNSS 850 860 870 880 890 900 IPFELSSYTN DKILIIYFNR LYKKIKDSSI LDMRYENNKF IDISGYGSNI SINGNVYIYS 910 920 930 940 950 960 TNRNQFGIYN SRLSEVNIAQ NNDIIYNSRY QNFSISFWVR IPKHYKPMNH NREYTIINCM 970 980 990 1000 1010 1020 GNNNSGWKIS LRTVRDCEII WTLQDTSGNK ENLIFRYEEL NRISNYINKW IFVTITNNRL 1030 1040 1050 1060 1070 1080 GNSRIYINGN LIVEKSISNL GDIHVSDNIL FKIVGCDDET YVGIRYFKVF NTELDKTEIE 1090 1100 1110 1120 1130 1140 TLYSNEPDPS ILKNYWGNYL LYNKKYYLFN LLRKDKYITL NSGILNINQQ RGVTEGSVFL 1150 1160 1170 1180 1190 1200 NYKLYEGVEV IIRKNGPIDI SNTDNFVRKN DLAYINVVDR GVEYRLYADT KSEKEKIIRT 1210 1220 1230 1240 1250 1260 SNLNDSLGQI IVMDSIGNNC TMNFQNNNGS NIGLLGFHSN NLVASSWYYN NIRRNTSSNG 1270 CFWSSISKEN GWKE

References

[1]	"Sequence of the gene encoding type F neurotoxin of Clostridium botulinum." East A.K., Richardson P.T., Allaway D., Collins M.D., Roberts T.A., Thompson D.E. FEMS Microbiol. Lett. 75:225-230(1992) [PubMed: 1398040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Type F / ATCC 23387.
[2]	"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." East A.K., Collins M.D. Curr. Microbiol. 29:69-77(1994) [PubMed: 7764998] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64. Strain: Type F / Hobbs FT10.
[3]	"Gene probes for identification of the botulinal neurotoxin gene and specific identification of neurotoxin types B, E, and F." Campbell K.D., Collins M.D., East A.K. J. Clin. Microbiol. 31:2255-2262(1993) [PubMed: 8408542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-1002.
[4]	"Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin." Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F., Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H. J. Biol. Chem. 269:12764-12772(1994) [PubMed: 8175689] [Abstract] Cited for: IDENTIFICATION OF SUBSTRATE.
+	Additional computationally mapped references.

Web resources

BotDB - A Database Resource for Clostridial Neurotoxins

Cross-references

Sequence databases

EMBLGenBankDDBJ

M92906 Genomic DNA. Translation: AAA23263.1.
S73676 Genomic DNA. Translation: AAC60475.1.
X70820 Genomic DNA. Translation: CAA50151.1.
X70816 Genomic DNA. Translation: CAA50147.1.

PIR

I40813.
S48109.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A8A	X-ray	2.00	A	1-436	[»]
2A97	X-ray	1.80	A/B	1-439	[»]

ModBase

Search...

Protein family/group databases

MEROPS

M27.002.

Enzyme and pathway databases

BRENDA

3.4.24.69. 19133.

Pathway_Interaction_DB

botulinumtoxinpathway. Effects of Botulinum toxin.

Reactome

REACT_11184. Botulinum neurotoxicity.

Family and domain databases

InterPro

IPR013320. ConA-like_subgrp.
IPR006025. Pept_M_Zn_BS.
IPR000395. Peptidase_M27.
IPR013104. Toxin_rcpt_bd_C.
IPR012928. Toxin_rcpt_bd_N.
IPR012500. Toxin_trans.
[Graphical view]

Gene3D

G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
G3DSA:3.90.1240.10. Peptidase_M27. 1 hit.

Pfam

PF01742. Peptidase_M27. 1 hit.
PF07951. Toxin_R_bind_C. 1 hit.
PF07953. Toxin_R_bind_N. 1 hit.
PF07952. Toxin_trans. 1 hit.
[Graphical view]

PRINTS

PR00760. BONTOXILYSIN.

ProDom

PD001963. Botulinum. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BXF_CLOBO

Accession

Primary (citable) accession number: P30996

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)