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Botulinum neurotoxin type G (BoNT/G) (EC 3.4.24.69) (Bontoxilysin-G) [Cleaved into: Botulinum neurotoxin G light chain; Botulinum neurotoxin G heavy chain]

 BXG_CLOBO               Reviewed;        1297 AA.
Q60393;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 122.
RecName: Full=Botulinum neurotoxin type G;
Short=BoNT/G;
EC=3.4.24.69;
AltName: Full=Bontoxilysin-G;
Contains:
RecName: Full=Botulinum neurotoxin G light chain;
Contains:
RecName: Full=Botulinum neurotoxin G heavy chain;
Flags: Precursor;
Name=botG;
Clostridium botulinum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1491;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Type G / 113 / 30;
PubMed=8268233; DOI=10.1016/0167-4781(93)90020-E;
Campbell K., Collins M.D., East A.K.;
"Nucleotide sequence of the gene coding for Clostridium botulinum
(Clostridium argentinense) type G neurotoxin: genealogical comparison
with other clostridial neurotoxins.";
Biochim. Biophys. Acta 1216:487-491(1993).
-!- 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.
-!- CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the
neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No
detected action on small molecule substrates.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: 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: Secreted {ECO:0000250}.
-!- MISCELLANEOUS: There are seven antigenically distinct forms of
botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
-!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial
Neurotoxins;
URL="https://botdb.abcc.ncifcrf.gov/";
-----------------------------------------------------------------------
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EMBL; X74162; CAA52275.1; -; Genomic_DNA.
PIR; S39791; S39791.
PDB; 1ZB7; X-ray; 2.35 A; A=1-443.
PDB; 2VXR; X-ray; 1.90 A; A=863-1297.
PDB; 3MPP; X-ray; 1.98 A; G=867-1297.
PDBsum; 1ZB7; -.
PDBsum; 2VXR; -.
PDBsum; 3MPP; -.
SMR; Q60393; -.
DIP; DIP-60790N; -.
IntAct; Q60393; 3.
MINT; Q60393; -.
MEROPS; M27.002; -.
BRENDA; 3.4.24.69; 1462.
Reactome; R-HSA-5250989; Toxicity of botulinum toxin type G (BoNT/G).
EvolutionaryTrace; Q60393; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004222; F:metalloendopeptidase activity; EXP:Reactome.
GO; GO:0008320; F:protein transmembrane transporter activity; TAS:Reactome.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0051609; P:inhibition of neurotransmitter uptake; IEA:InterPro.
Gene3D; 1.20.1120.10; -; 2.
InterPro; IPR000395; Bot/tetX.
InterPro; IPR036248; Clostridium_toxin_transloc.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
InterPro; IPR013104; Toxin_rcpt-bd_C.
InterPro; IPR012928; Toxin_rcpt-bd_N.
InterPro; IPR012500; Toxin_trans.
Pfam; PF01742; Peptidase_M27; 1.
Pfam; PF07951; Toxin_R_bind_C; 1.
Pfam; PF07953; Toxin_R_bind_N; 1.
Pfam; PF07952; Toxin_trans; 1.
PRINTS; PR00760; BONTOXILYSIN.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF50386; SSF50386; 1.
SUPFAM; SSF58091; SSF58091; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Disulfide bond; Hydrolase; Metal-binding;
Metalloprotease; Neurotoxin; Protease; Secreted; Toxin; Virulence;
Zinc.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 442 Botulinum neurotoxin G light chain.
/FTId=PRO_0000029227.
CHAIN 443 1297 Botulinum neurotoxin G heavy chain.
/FTId=PRO_0000029228.
ACT_SITE 231 231 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 230 230 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 234 234 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
DISULFID 436 450 Interchain (between light and heavy
chains). {ECO:0000305}.
STRAND 16 23 {ECO:0000244|PDB:1ZB7}.
STRAND 28 30 {ECO:0000244|PDB:1ZB7}.
STRAND 34 40 {ECO:0000244|PDB:1ZB7}.
STRAND 43 46 {ECO:0000244|PDB:1ZB7}.
STRAND 69 74 {ECO:0000244|PDB:1ZB7}.
TURN 76 79 {ECO:0000244|PDB:1ZB7}.
HELIX 82 99 {ECO:0000244|PDB:1ZB7}.
HELIX 103 114 {ECO:0000244|PDB:1ZB7}.
TURN 134 136 {ECO:0000244|PDB:1ZB7}.
STRAND 137 142 {ECO:0000244|PDB:1ZB7}.
STRAND 150 155 {ECO:0000244|PDB:1ZB7}.
STRAND 157 161 {ECO:0000244|PDB:1ZB7}.
STRAND 171 173 {ECO:0000244|PDB:1ZB7}.
HELIX 182 184 {ECO:0000244|PDB:1ZB7}.
STRAND 185 187 {ECO:0000244|PDB:1ZB7}.
STRAND 191 194 {ECO:0000244|PDB:1ZB7}.
STRAND 199 208 {ECO:0000244|PDB:1ZB7}.
STRAND 215 221 {ECO:0000244|PDB:1ZB7}.
HELIX 224 239 {ECO:0000244|PDB:1ZB7}.
HELIX 266 273 {ECO:0000244|PDB:1ZB7}.
TURN 277 279 {ECO:0000244|PDB:1ZB7}.
HELIX 282 303 {ECO:0000244|PDB:1ZB7}.
STRAND 308 313 {ECO:0000244|PDB:1ZB7}.
HELIX 316 327 {ECO:0000244|PDB:1ZB7}.
HELIX 341 353 {ECO:0000244|PDB:1ZB7}.
HELIX 357 364 {ECO:0000244|PDB:1ZB7}.
STRAND 377 381 {ECO:0000244|PDB:1ZB7}.
TURN 388 390 {ECO:0000244|PDB:1ZB7}.
TURN 393 395 {ECO:0000244|PDB:1ZB7}.
HELIX 400 402 {ECO:0000244|PDB:1ZB7}.
HELIX 406 411 {ECO:0000244|PDB:1ZB7}.
TURN 413 415 {ECO:0000244|PDB:1ZB7}.
HELIX 417 419 {ECO:0000244|PDB:1ZB7}.
TURN 425 427 {ECO:0000244|PDB:1ZB7}.
STRAND 428 432 {ECO:0000244|PDB:1ZB7}.
STRAND 870 876 {ECO:0000244|PDB:2VXR}.
STRAND 879 882 {ECO:0000244|PDB:2VXR}.
STRAND 889 892 {ECO:0000244|PDB:2VXR}.
STRAND 897 899 {ECO:0000244|PDB:2VXR}.
STRAND 905 911 {ECO:0000244|PDB:2VXR}.
STRAND 916 919 {ECO:0000244|PDB:2VXR}.
TURN 922 924 {ECO:0000244|PDB:2VXR}.
STRAND 927 930 {ECO:0000244|PDB:2VXR}.
STRAND 933 940 {ECO:0000244|PDB:2VXR}.
HELIX 946 948 {ECO:0000244|PDB:2VXR}.
HELIX 949 954 {ECO:0000244|PDB:2VXR}.
STRAND 956 964 {ECO:0000244|PDB:2VXR}.
STRAND 967 974 {ECO:0000244|PDB:2VXR}.
STRAND 977 983 {ECO:0000244|PDB:2VXR}.
STRAND 989 995 {ECO:0000244|PDB:2VXR}.
STRAND 998 1002 {ECO:0000244|PDB:3MPP}.
STRAND 1010 1016 {ECO:0000244|PDB:2VXR}.
STRAND 1020 1026 {ECO:0000244|PDB:2VXR}.
STRAND 1029 1035 {ECO:0000244|PDB:2VXR}.
STRAND 1046 1054 {ECO:0000244|PDB:2VXR}.
STRAND 1061 1072 {ECO:0000244|PDB:2VXR}.
HELIX 1076 1086 {ECO:0000244|PDB:2VXR}.
STRAND 1097 1099 {ECO:0000244|PDB:2VXR}.
STRAND 1105 1113 {ECO:0000244|PDB:2VXR}.
STRAND 1116 1121 {ECO:0000244|PDB:2VXR}.
HELIX 1122 1124 {ECO:0000244|PDB:2VXR}.
STRAND 1126 1131 {ECO:0000244|PDB:2VXR}.
STRAND 1134 1136 {ECO:0000244|PDB:2VXR}.
STRAND 1141 1143 {ECO:0000244|PDB:2VXR}.
STRAND 1150 1155 {ECO:0000244|PDB:2VXR}.
STRAND 1174 1184 {ECO:0000244|PDB:2VXR}.
STRAND 1186 1191 {ECO:0000244|PDB:2VXR}.
STRAND 1196 1200 {ECO:0000244|PDB:2VXR}.
STRAND 1202 1206 {ECO:0000244|PDB:2VXR}.
STRAND 1216 1219 {ECO:0000244|PDB:2VXR}.
STRAND 1229 1236 {ECO:0000244|PDB:2VXR}.
STRAND 1239 1248 {ECO:0000244|PDB:2VXR}.
STRAND 1260 1267 {ECO:0000244|PDB:2VXR}.
HELIX 1268 1272 {ECO:0000244|PDB:2VXR}.
STRAND 1275 1277 {ECO:0000244|PDB:2VXR}.
STRAND 1286 1289 {ECO:0000244|PDB:2VXR}.
SEQUENCE 1297 AA; 149146 MW; 306CF54CF3973C3B CRC64;
MPVNIKXFNY NDPINNDDII MMEPFNDPGP GTYYKAFRII DRIWIVPERF TYGFQPDQFN
ASTGVFSKDV YEYYDPTYLK TDAEKDKFLK TMIKLFNRIN SKPSGQRLLD MIVDAIPYLG
NASTPPDKFA ANVANVSINK KIIQPGAEDQ IKGLMTNLII FGPGPVLSDN FTDSMIMNGH
SPISEGFGAR MMIRFCPSCL NVFNNVQENK DTSIFSRRAY FADPALTLMH ELIHVLHGLY
GIKISNLPIT PNTKEFFMQH SDPVQAEELY TFGGHDPSVI SPSTDMNIYN KALQNFQDIA
NRLNIVSSAQ GSGIDISLYK QIYKNKYDFV EDPNGKYSVD KDKFDKLYKA LMFGFTETNL
AGEYGIKTRY SYFSEYLPPI KTEKLLDNTI YTQNEGFNIA SKNLKTEFNG QNKAVNKEAY
EEISLEHLVI YRIAMCKPVM YKNTGKSEQC IIVNNEDLFF IANKDSFSKD LAKAETIAYN
TQNNTIENNF SIDQLILDND LSSGIDLPNE NTEPFTNFDD IDIPVYIKQS ALKKIFVDGD
SLFEYLHAQT FPSNIENLQL TNSLNDALRN NNKVYTFFST NLVEKANTVV GASLFVNWVK
GVIDDFTSES TQKSTIDKVS DVSIIIPYIG PALNVGNETA KENFKNAFEI GGAAILMEFI
PELIVPIVGF FTLESYVGNK GHIIMTISNA LKKRDQKWTD MYGLIVSQWL STVNTQFYTI
KERMYNALNN QSQAIEKIIE DQYNRYSEED KMNINIDFND IDFKLNQSIN LAINNIDDFI
NQCSISYLMN RMIPLAVKKL KDFDDNLKRD LLEYIDTNEL YLLDEVNILK SKVNRHLKDS
IPFDLSLYTK DTILIQVFNN YISNISSNAI LSLSYRGGRL IDSSGYGATM NVGSDVIFND
IGNGQFKLNN SENSNITAHQ SKFVVYDSMF DNFSINFWVR TPKYNNNDIQ TYLQNEYTII
SCIKNDSGWK VSIKGNRIIW TLIDVNAKSK SIFFEYSIKD NISDYINKWF SITITNDRLG
NANIYINGSL KKSEKILNLD RINSSNDIDF KLINCTDTTK FVWIKDFNIF GRELNATEVS
SLYWIQSSTN TLKDFWGNPL RYDTQYYLFN QGMQNIYIKY FSKASMGETA PRTNFNNAAI
NYQNLYLGLR FIIKKASNSR NINNDNIVRE GDYIYLNIDN ISDESYRVYV LVNSKEIQTQ
LFLAPINDDP TFYDVLQIKK YYEKTTYNCQ ILCEKDTKTF GLFGIGKFVK DYGYVWDTYD
NYFCISQWYL RRISENINKL RLGCNWQFIP VDEGWTE


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