Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi230Zinc; catalyticPROSITE-ProRule annotation1
Active sitei231PROSITE-ProRule annotation1
Metal bindingi234Zinc; 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-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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000292272 – 442Botulinum neurotoxin G light chainAdd BLAST441
ChainiPRO_0000029228443 – 1297Botulinum neurotoxin G heavy chainAdd BLAST855

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactor.
MINTiMINT-8302082.

Structurei

Secondary structure

11297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 23Combined sources8
Beta strandi28 – 30Combined sources3
Beta strandi34 – 40Combined sources7
Beta strandi43 – 46Combined sources4
Beta strandi69 – 74Combined sources6
Turni76 – 79Combined sources4
Helixi82 – 99Combined sources18
Helixi103 – 114Combined sources12
Turni134 – 136Combined sources3
Beta strandi137 – 142Combined sources6
Beta strandi150 – 155Combined sources6
Beta strandi157 – 161Combined sources5
Beta strandi171 – 173Combined sources3
Helixi182 – 184Combined sources3
Beta strandi185 – 187Combined sources3
Beta strandi191 – 194Combined sources4
Beta strandi199 – 208Combined sources10
Beta strandi215 – 221Combined sources7
Helixi224 – 239Combined sources16
Helixi266 – 273Combined sources8
Turni277 – 279Combined sources3
Helixi282 – 303Combined sources22
Beta strandi308 – 313Combined sources6
Helixi316 – 327Combined sources12
Helixi341 – 353Combined sources13
Helixi357 – 364Combined sources8
Beta strandi377 – 381Combined sources5
Turni388 – 390Combined sources3
Turni393 – 395Combined sources3
Helixi400 – 402Combined sources3
Helixi406 – 411Combined sources6
Turni413 – 415Combined sources3
Helixi417 – 419Combined sources3
Turni425 – 427Combined sources3
Beta strandi428 – 432Combined sources5
Beta strandi870 – 876Combined sources7
Beta strandi879 – 882Combined sources4
Beta strandi889 – 892Combined sources4
Beta strandi897 – 899Combined sources3
Beta strandi905 – 911Combined sources7
Beta strandi916 – 919Combined sources4
Turni922 – 924Combined sources3
Beta strandi927 – 930Combined sources4
Beta strandi933 – 940Combined sources8
Helixi946 – 948Combined sources3
Helixi949 – 954Combined sources6
Beta strandi956 – 964Combined sources9
Beta strandi967 – 974Combined sources8
Beta strandi977 – 983Combined sources7
Beta strandi989 – 995Combined sources7
Beta strandi998 – 1002Combined sources5
Beta strandi1010 – 1016Combined sources7
Beta strandi1020 – 1026Combined sources7
Beta strandi1029 – 1035Combined sources7
Beta strandi1046 – 1054Combined sources9
Beta strandi1061 – 1072Combined sources12
Helixi1076 – 1086Combined sources11
Beta strandi1097 – 1099Combined sources3
Beta strandi1105 – 1113Combined sources9
Beta strandi1116 – 1121Combined sources6
Helixi1122 – 1124Combined sources3
Beta strandi1126 – 1131Combined sources6
Beta strandi1134 – 1136Combined sources3
Beta strandi1141 – 1143Combined sources3
Beta strandi1150 – 1155Combined sources6
Beta strandi1174 – 1184Combined sources11
Beta strandi1186 – 1191Combined sources6
Beta strandi1196 – 1200Combined sources5
Beta strandi1202 – 1206Combined sources5
Beta strandi1216 – 1219Combined sources4
Beta strandi1229 – 1236Combined sources8
Beta strandi1239 – 1248Combined sources10
Beta strandi1260 – 1267Combined sources8
Helixi1268 – 1272Combined sources5
Beta strandi1275 – 1277Combined sources3
Beta strandi1286 – 1289Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZB7X-ray2.35A1-443[»]
2VXRX-ray1.90A863-1297[»]
3MPPX-ray1.98G867-1297[»]
SMRiQ60393.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZB7X-ray2.35A1-443[»]
2VXRX-ray1.90A863-1297[»]
3MPPX-ray1.98G867-1297[»]
SMRiQ60393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60790N.
IntActiQ60393. 1 interactor.
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...

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: November 2, 2016
This is version 114 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.