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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)DescriptionActionsGraphical viewLength
Metal bindingi227Zinc; catalyticPROSITE-ProRule annotation1
Active sitei228PROSITE-ProRule annotation1
Metal bindingi231Zinc; catalyticPROSITE-ProRule annotation1

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 databases

ChEMBLiCHEMBL2007627.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000292251 – 436Botulinum neurotoxin F light chainAdd BLAST436
ChainiPRO_0000029226437 – 1274Botulinum neurotoxin F heavy chainAdd BLAST838

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactors.

Chemistry databases

BindingDBiP30996.

Structurei

Secondary structure

11274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 22Combined sources7
Helixi28 – 30Combined sources3
Beta strandi34 – 40Combined sources7
Beta strandi43 – 49Combined sources7
Helixi56 – 59Combined sources4
Beta strandi69 – 71Combined sources3
Turni75 – 78Combined sources4
Helixi81 – 98Combined sources18
Helixi102 – 113Combined sources12
Turni133 – 135Combined sources3
Beta strandi136 – 140Combined sources5
Beta strandi146 – 150Combined sources5
Beta strandi152 – 157Combined sources6
Beta strandi166 – 169Combined sources4
Helixi182 – 184Combined sources3
Beta strandi185 – 187Combined sources3
Beta strandi191 – 194Combined sources4
Beta strandi199 – 203Combined sources5
Beta strandi216 – 218Combined sources3
Helixi221 – 236Combined sources16
Turni241 – 245Combined sources5
Beta strandi247 – 251Combined sources5
Turni253 – 256Combined sources4
Beta strandi259 – 263Combined sources5
Helixi264 – 270Combined sources7
Helixi272 – 277Combined sources6
Helixi280 – 303Combined sources24
Helixi313 – 323Combined sources11
Beta strandi326 – 328Combined sources3
Beta strandi334 – 336Combined sources3
Helixi338 – 348Combined sources11
Helixi353 – 360Combined sources8
Beta strandi366 – 369Combined sources4
Beta strandi374 – 376Combined sources3
Turni383 – 385Combined sources3
Turni388 – 390Combined sources3
Helixi395 – 404Combined sources10
Turni406 – 408Combined sources3
Helixi410 – 412Combined sources3

3D structure databases

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

Protein-protein interaction databases

IntActiP30996. 2 interactors.

Chemistry databases

BindingDBiP30996.
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...

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: November 2, 2016
This is version 137 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.