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Protein

Botulinum neurotoxin type G

Gene

botG

Organism
Clostridium botulinum
Status
Reviewed-Annotation score: Annotation score: 4 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.

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 bindingi230 – 2301Zinc; catalyticPROSITE-ProRule annotation
Active sitei231 – 2311PROSITE-ProRule annotation
Metal bindingi234 – 2341Zinc; 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-5250989. Toxicity of botulinum toxin type G (BoNT/G).

Protein family/group databases

MEROPSiM27.002.

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 442441Botulinum neurotoxin G light chainPRO_0000029227Add
BLAST
Chaini443 – 1297855Botulinum neurotoxin G heavy chainPRO_0000029228Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi436 ↔ 450Interchain (between light and heavy chains)Curated

Keywords - PTMi

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

DIPiDIP-60790N.
IntActiQ60393. 1 interaction.
MINTiMINT-8302082.

Structurei

Secondary structure

1
1297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 238Combined sources
Beta strandi28 – 303Combined sources
Beta strandi34 – 407Combined sources
Beta strandi43 – 464Combined sources
Beta strandi69 – 746Combined sources
Turni76 – 794Combined sources
Helixi82 – 9918Combined sources
Helixi103 – 11412Combined sources
Turni134 – 1363Combined sources
Beta strandi137 – 1426Combined sources
Beta strandi150 – 1556Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi171 – 1733Combined sources
Helixi182 – 1843Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi191 – 1944Combined sources
Beta strandi199 – 20810Combined sources
Beta strandi215 – 2217Combined sources
Helixi224 – 23916Combined sources
Helixi266 – 2738Combined sources
Turni277 – 2793Combined sources
Helixi282 – 30322Combined sources
Beta strandi308 – 3136Combined sources
Helixi316 – 32712Combined sources
Helixi341 – 35313Combined sources
Helixi357 – 3648Combined sources
Beta strandi377 – 3815Combined sources
Turni388 – 3903Combined sources
Turni393 – 3953Combined sources
Helixi400 – 4023Combined sources
Helixi406 – 4116Combined sources
Turni413 – 4153Combined sources
Helixi417 – 4193Combined sources
Turni425 – 4273Combined sources
Beta strandi428 – 4325Combined sources
Beta strandi870 – 8767Combined sources
Beta strandi879 – 8824Combined sources
Beta strandi889 – 8924Combined sources
Beta strandi897 – 8993Combined sources
Beta strandi905 – 9117Combined sources
Beta strandi916 – 9194Combined sources
Turni922 – 9243Combined sources
Beta strandi927 – 9304Combined sources
Beta strandi933 – 9408Combined sources
Helixi946 – 9483Combined sources
Helixi949 – 9546Combined sources
Beta strandi956 – 9649Combined sources
Beta strandi967 – 9748Combined sources
Beta strandi977 – 9837Combined sources
Beta strandi989 – 9957Combined sources
Beta strandi998 – 10025Combined sources
Beta strandi1010 – 10167Combined sources
Beta strandi1020 – 10267Combined sources
Beta strandi1029 – 10357Combined sources
Beta strandi1046 – 10549Combined sources
Beta strandi1061 – 107212Combined sources
Helixi1076 – 108611Combined sources
Beta strandi1097 – 10993Combined sources
Beta strandi1105 – 11139Combined sources
Beta strandi1116 – 11216Combined sources
Helixi1122 – 11243Combined sources
Beta strandi1126 – 11316Combined sources
Beta strandi1134 – 11363Combined sources
Beta strandi1141 – 11433Combined sources
Beta strandi1150 – 11556Combined sources
Beta strandi1174 – 118411Combined sources
Beta strandi1186 – 11916Combined sources
Beta strandi1196 – 12005Combined sources
Beta strandi1202 – 12065Combined sources
Beta strandi1216 – 12194Combined sources
Beta strandi1229 – 12368Combined sources
Beta strandi1239 – 124810Combined sources
Beta strandi1260 – 12678Combined sources
Helixi1268 – 12725Combined sources
Beta strandi1275 – 12773Combined sources
Beta strandi1286 – 12894Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZB7X-ray2.35A1-443[»]
2VXRX-ray1.90A863-1297[»]
3MPPX-ray1.98G867-1297[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60393.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

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.

Q60393-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVNIKXFNY NDPINNDDII MMEPFNDPGP GTYYKAFRII DRIWIVPERF
60 70 80 90 100
TYGFQPDQFN ASTGVFSKDV YEYYDPTYLK TDAEKDKFLK TMIKLFNRIN
110 120 130 140 150
SKPSGQRLLD MIVDAIPYLG NASTPPDKFA ANVANVSINK KIIQPGAEDQ
160 170 180 190 200
IKGLMTNLII FGPGPVLSDN FTDSMIMNGH SPISEGFGAR MMIRFCPSCL
210 220 230 240 250
NVFNNVQENK DTSIFSRRAY FADPALTLMH ELIHVLHGLY GIKISNLPIT
260 270 280 290 300
PNTKEFFMQH SDPVQAEELY TFGGHDPSVI SPSTDMNIYN KALQNFQDIA
310 320 330 340 350
NRLNIVSSAQ GSGIDISLYK QIYKNKYDFV EDPNGKYSVD KDKFDKLYKA
360 370 380 390 400
LMFGFTETNL AGEYGIKTRY SYFSEYLPPI KTEKLLDNTI YTQNEGFNIA
410 420 430 440 450
SKNLKTEFNG QNKAVNKEAY EEISLEHLVI YRIAMCKPVM YKNTGKSEQC
460 470 480 490 500
IIVNNEDLFF IANKDSFSKD LAKAETIAYN TQNNTIENNF SIDQLILDND
510 520 530 540 550
LSSGIDLPNE NTEPFTNFDD IDIPVYIKQS ALKKIFVDGD SLFEYLHAQT
560 570 580 590 600
FPSNIENLQL TNSLNDALRN NNKVYTFFST NLVEKANTVV GASLFVNWVK
610 620 630 640 650
GVIDDFTSES TQKSTIDKVS DVSIIIPYIG PALNVGNETA KENFKNAFEI
660 670 680 690 700
GGAAILMEFI PELIVPIVGF FTLESYVGNK GHIIMTISNA LKKRDQKWTD
710 720 730 740 750
MYGLIVSQWL STVNTQFYTI KERMYNALNN QSQAIEKIIE DQYNRYSEED
760 770 780 790 800
KMNINIDFND IDFKLNQSIN LAINNIDDFI NQCSISYLMN RMIPLAVKKL
810 820 830 840 850
KDFDDNLKRD LLEYIDTNEL YLLDEVNILK SKVNRHLKDS IPFDLSLYTK
860 870 880 890 900
DTILIQVFNN YISNISSNAI LSLSYRGGRL IDSSGYGATM NVGSDVIFND
910 920 930 940 950
IGNGQFKLNN SENSNITAHQ SKFVVYDSMF DNFSINFWVR TPKYNNNDIQ
960 970 980 990 1000
TYLQNEYTII SCIKNDSGWK VSIKGNRIIW TLIDVNAKSK SIFFEYSIKD
1010 1020 1030 1040 1050
NISDYINKWF SITITNDRLG NANIYINGSL KKSEKILNLD RINSSNDIDF
1060 1070 1080 1090 1100
KLINCTDTTK FVWIKDFNIF GRELNATEVS SLYWIQSSTN TLKDFWGNPL
1110 1120 1130 1140 1150
RYDTQYYLFN QGMQNIYIKY FSKASMGETA PRTNFNNAAI NYQNLYLGLR
1160 1170 1180 1190 1200
FIIKKASNSR NINNDNIVRE GDYIYLNIDN ISDESYRVYV LVNSKEIQTQ
1210 1220 1230 1240 1250
LFLAPINDDP TFYDVLQIKK YYEKTTYNCQ ILCEKDTKTF GLFGIGKFVK
1260 1270 1280 1290
DYGYVWDTYD NYFCISQWYL RRISENINKL RLGCNWQFIP VDEGWTE
Length:1,297
Mass (Da):149,146
Last modified:January 23, 2007 - v2
Checksum:i306CF54CF3973C3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74162 Genomic DNA. Translation: CAA52275.1.
PIRiS39791.

Cross-referencesi

Web resourcesi

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74162 Genomic DNA. Translation: CAA52275.1.
PIRiS39791.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZB7X-ray2.35A1-443[»]
2VXRX-ray1.90A863-1297[»]
3MPPX-ray1.98G867-1297[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60790N.
IntActiQ60393. 1 interaction.
MINTiMINT-8302082.

Protein family/group databases

MEROPSiM27.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250989. Toxicity of botulinum toxin type G (BoNT/G).

Miscellaneous databases

EvolutionaryTraceiQ60393.

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. "Nucleotide sequence of the gene coding for Clostridium botulinum (Clostridium argentinense) type G neurotoxin: genealogical comparison with other clostridial neurotoxins."
    Campbell K., Collins M.D., East A.K.
    Biochim. Biophys. Acta 1216:487-491(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Type G / 113 / 30.

Entry informationi

Entry nameiBXG_CLOBO
AccessioniPrimary (citable) accession number: Q60393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 112 of the entry and version 2 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.