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Protein

Botulinum neurotoxin type F

Gene

botF

Organism
Clostridium botulinum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi227 – 2271Zinc; catalyticPROSITE-ProRule annotation
Active sitei228 – 2281PROSITE-ProRule annotation
Metal bindingi231 – 2311Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250981. Toxicity of botulinum toxin type F (BoNT/F).

Protein family/group databases

MEROPSiM27.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Botulinum neurotoxin type F (EC:3.4.24.69)
Short name:
BoNT/F
Alternative name(s):
Bontoxilysin-F
Cleaved into the following 2 chains:
Gene namesi
Name:botF
OrganismiClostridium botulinum
Taxonomic identifieri1491 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell junction, Host cell membrane, Host cytoplasm, Host membrane, Host synapse, Membrane, Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2007627.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Botulinum neurotoxin F light chainPRO_0000029225Add
BLAST
Chaini437 – 1274838Botulinum neurotoxin F heavy chainPRO_0000029226Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi429 ↔ 445Interchain (between light and heavy chains)Curated

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

IntActiP30996. 2 interactions.

Structurei

Secondary structure

1
1274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 227Combined sources
Helixi28 – 303Combined sources
Beta strandi34 – 407Combined sources
Beta strandi43 – 497Combined sources
Helixi56 – 594Combined sources
Beta strandi69 – 713Combined sources
Turni75 – 784Combined sources
Helixi81 – 9818Combined sources
Helixi102 – 11312Combined sources
Turni133 – 1353Combined sources
Beta strandi136 – 1405Combined sources
Beta strandi146 – 1505Combined sources
Beta strandi152 – 1576Combined sources
Beta strandi166 – 1694Combined sources
Helixi182 – 1843Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi191 – 1944Combined sources
Beta strandi199 – 2035Combined sources
Beta strandi216 – 2183Combined sources
Helixi221 – 23616Combined sources
Turni241 – 2455Combined sources
Beta strandi247 – 2515Combined sources
Turni253 – 2564Combined sources
Beta strandi259 – 2635Combined sources
Helixi264 – 2707Combined sources
Helixi272 – 2776Combined sources
Helixi280 – 30324Combined sources
Helixi313 – 32311Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi334 – 3363Combined sources
Helixi338 – 34811Combined sources
Helixi353 – 3608Combined sources
Beta strandi366 – 3694Combined sources
Beta strandi374 – 3763Combined sources
Turni383 – 3853Combined sources
Turni388 – 3903Combined sources
Helixi395 – 40410Combined sources
Turni406 – 4083Combined sources
Helixi410 – 4123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A8AX-ray2.00A1-439[»]
2A97X-ray1.80A/B1-439[»]
3FIEX-ray2.10A/B5-419[»]
3FIIX-ray2.17A5-419[»]
ProteinModelPortaliP30996.
SMRiP30996. Positions 2-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30996.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

Keywords - Domaini

Transmembrane

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
IPR013104. Toxin_rcpt-bd_C.
IPR012928. Toxin_rcpt-bd_N.
IPR012500. Toxin_trans.
[Graphical view]
PfamiPF01742. 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]
PRINTSiPR00760. BONTOXILYSIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50386. SSF50386. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30996-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVAINSFNY NDPVNDDTIL YMQIPYEEKS KKYYKAFEIM RNVWIIPERN
60 70 80 90 100
TIGTNPSDFD PPASLKNGSS AYYDPNYLTT DAEKDRYLKT TIKLFKRINS
110 120 130 140 150
NPAGKVLLQE ISYAKPYLGN DHTPIDEFSP VTRTTSVNIK LSTNVESSML
160 170 180 190 200
LNLLVLGAGP DIFESCCYPV RKLIDPDVVY DPSNYGFGSI NIVTFSPEYE
210 220 230 240 250
YTFNDISGGH NSSTESFIAD PAISLAHELI HALHGLYGAR GVTYEETIEV
260 270 280 290 300
KQAPLMIAEK PIRLEEFLTF GGQDLNIITS AMKEKIYNNL LANYEKIATR
310 320 330 340 350
LSEVNSAPPE YDINEYKDYF QWKYGLDKNA DGSYTVNENK FNEIYKKLYS
360 370 380 390 400
FTESDLANKF KVKCRNTYFI KYEFLKVPNL LDDDIYTVSE GFNIGNLAVN
410 420 430 440 450
NRGQSIKLNP KIIDSIPDKG LVEKIVKFCK SVIPRKGTKA PPRLCIRVNN
460 470 480 490 500
SELFFVASES SYNENDINTP KEIDDTTNLN NNYRNNLDEV ILDYNSQTIP
510 520 530 540 550
QISNRTLNTL VQDNSYVPRY DSNGTSEIEE YDVVDFNVFF YLHAQKVPEG
560 570 580 590 600
ETNISLTSSI DTALLEESKD IFFSSEFIDT INKPVNAALF IDWISKVIRD
610 620 630 640 650
FTTEATQKST VDKIADISLI VPYVGLALNI IIEAEKGNFE EAFELLGVGI
660 670 680 690 700
LLEFVPELTI PVILVFTIKS YIDSYENKNK AIKAINNSLI EREAKWKEIY
710 720 730 740 750
SWIVSNWLTR INTQFNKRKE QMYQALQNQV DAIKTAIEYK YNNYTSDEKN
760 770 780 790 800
RLESEYNINN IEEELNKKVS LAMKNIERFM TESSISYLMK LINEAKVGKL
810 820 830 840 850
KKYDNHVKSD LLNYILDHRS ILGEQTNELS DLVTSTLNSS IPFELSSYTN
860 870 880 890 900
DKILIIYFNR LYKKIKDSSI LDMRYENNKF IDISGYGSNI SINGNVYIYS
910 920 930 940 950
TNRNQFGIYN SRLSEVNIAQ NNDIIYNSRY QNFSISFWVR IPKHYKPMNH
960 970 980 990 1000
NREYTIINCM GNNNSGWKIS LRTVRDCEII WTLQDTSGNK ENLIFRYEEL
1010 1020 1030 1040 1050
NRISNYINKW IFVTITNNRL GNSRIYINGN LIVEKSISNL GDIHVSDNIL
1060 1070 1080 1090 1100
FKIVGCDDET YVGIRYFKVF NTELDKTEIE TLYSNEPDPS ILKNYWGNYL
1110 1120 1130 1140 1150
LYNKKYYLFN LLRKDKYITL NSGILNINQQ RGVTEGSVFL NYKLYEGVEV
1160 1170 1180 1190 1200
IIRKNGPIDI SNTDNFVRKN DLAYINVVDR GVEYRLYADT KSEKEKIIRT
1210 1220 1230 1240 1250
SNLNDSLGQI IVMDSIGNNC TMNFQNNNGS NIGLLGFHSN NLVASSWYYN
1260 1270
NIRRNTSSNG CFWSSISKEN GWKE
Length:1,274
Mass (Da):146,710
Last modified:July 1, 1993 - v1
Checksum:i5B99756A7438B921
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92906 Genomic DNA. Translation: AAA23263.1.
S73676 Genomic DNA. Translation: AAC60475.1.
X70820 Genomic DNA. Translation: CAA50151.1.
X70816 Genomic DNA. Translation: CAA50147.1.
PIRiI40813.
S48109.

Cross-referencesi

Web resourcesi

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92906 Genomic DNA. Translation: AAA23263.1.
S73676 Genomic DNA. Translation: AAC60475.1.
X70820 Genomic DNA. Translation: CAA50151.1.
X70816 Genomic DNA. Translation: CAA50147.1.
PIRiI40813.
S48109.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A8AX-ray2.00A1-439[»]
2A97X-ray1.80A/B1-439[»]
3FIEX-ray2.10A/B5-419[»]
3FIIX-ray2.17A5-419[»]
ProteinModelPortaliP30996.
SMRiP30996. Positions 2-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP30996. 2 interactions.

Chemistry

ChEMBLiCHEMBL2007627.

Protein family/group databases

MEROPSiM27.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250981. Toxicity of botulinum toxin type F (BoNT/F).

Miscellaneous databases

EvolutionaryTraceiP30996.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
IPR013104. Toxin_rcpt-bd_C.
IPR012928. Toxin_rcpt-bd_N.
IPR012500. Toxin_trans.
[Graphical view]
PfamiPF01742. 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]
PRINTSiPR00760. BONTOXILYSIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50386. SSF50386. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF SUBSTRATE.

Entry informationi

Entry nameiBXF_CLOBO
AccessioniPrimary (citable) accession number: P30996
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: March 16, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.