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

 BXA1_CLOBH              Reviewed;        1296 AA.
A5HZZ9; A7G1U9;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 1.
28-MAR-2018, entry version 89.
RecName: Full=Botulinum neurotoxin type A;
Short=BoNT/A;
EC=3.4.24.69;
AltName: Full=Bontoxilysin-A;
Short=BOTOX;
Contains:
RecName: Full=Botulinum neurotoxin A light chain;
Contains:
RecName: Full=Botulinum neurotoxin A heavy chain;
Flags: Precursor;
Name=botA; OrderedLocusNames=CBO0806, CLC_0862;
Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=441771;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
PubMed=17519437; DOI=10.1101/gr.6282807;
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J.,
Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T.,
Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N.,
Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E.,
Sanders M., Simmonds M., White B., Whithead S., Parkhill J.;
"Genome sequence of a proteolytic (Group I) Clostridium botulinum
strain Hall A and comparative analysis of the clostridial genomes.";
Genome Res. 17:1082-1092(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
PubMed=18060065; DOI=10.1371/journal.pone.0001271;
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-
A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
plasmids.";
PLoS ONE 2:E1271-E1271(2007).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
PubMed=2669749; DOI=10.1016/0006-291X(89)90828-0;
Betley M.J., Somers E., Dasgupta B.R.;
"Characterization of botulinum type A neurotoxin gene: delineation of
the N-terminal encoding region.";
Biochem. Biophys. Res. Commun. 162:1388-1395(1989).
[4]
PROTEIN SEQUENCE OF 867-880 AND 1148-1219.
PubMed=8397793; DOI=10.1007/BF01028197;
Gimenez J.A., DasGupta B.R.;
"Botulinum type A neurotoxin digested with pepsin yields 132, 97, 72,
45, 42, and 18 kD fragments.";
J. Protein Chem. 12:351-363(1993).
[5]
IDENTIFICATION OF SUBSTRATE.
PubMed=8294407;
Binz T., Blasi J., Yamasaki S., Baumeister A., Link E., Suedhof T.C.,
Jahn R., Niemann H.;
"Proteolysis of SNAP-25 by types E and A botulinal neurotoxins.";
J. Biol. Chem. 269:1617-1620(1994).
-!- FUNCTION: Inhibits acetylcholine release. The botulinum toxin
binds with high affinity to peripheral neuronal presynaptic
membrane to the secretory vesicle protein SV2. It binds directly
to the largest luminal loop of SV2A, SV2B and SV2C. It is then
internalized by receptor-mediated endocytosis. The C-terminus of
the heavy chain (H) is responsible for the adherence of the toxin
to the cell surface while the N-terminus mediates transport of the
light chain from the endocytic vesicle to the cytosol. After
translocation, the light chain (L) hydrolyzes the 197-Gln-|-Arg-
198 bond in SNAP-25, thereby blocking neurotransmitter release.
Inhibition of acetylcholine release results in flaccid paralysis,
with frequent heart or respiratory failure.
-!- 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;
Note=Binds 1 zinc ion per subunit.;
-!- SUBUNIT: Disulfide-linked heterodimer of a light chain (L) and a
heavy chain (H).
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin A light chain:
Secreted. Host cytoplasm, host cytosol.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin A heavy chain:
Secreted. Host cell junction, host synapse, host presynaptic cell
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- PHARMACEUTICAL: Available under the name BOTOX (Allergan) for the
treatment of strabismus and blepharospasm associated with dystonia
and cervical dystonia. Also used for the treatment of hemifacial
spasm and a number of other neurological disorders characterized
by abnormal muscle contraction.
-!- 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=BOTOX product information Web site;
URL="http://www.botox.com/";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=From sausages to
wrinkles - Issue 19 of February 2002;
URL="https://web.expasy.org/spotlight/back_issues/019";
-!- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial
Neurotoxins;
URL="https://botdb.abcc.ncifcrf.gov/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AM412317; CAL82360.1; -; Genomic_DNA.
EMBL; CP000727; ABS38337.1; -; Genomic_DNA.
PIR; A35294; BTCLAB.
RefSeq; WP_011948511.1; NC_009698.1.
RefSeq; YP_001253342.1; NC_009495.1.
RefSeq; YP_001386738.1; NC_009698.1.
PDB; 1XTF; X-ray; 2.20 A; A/B=2-420.
PDB; 1XTG; X-ray; 2.10 A; A=2-422.
PDB; 2W2D; X-ray; 2.59 A; A/C=1-442, B/D=447-877.
PDB; 3DSE; X-ray; 1.90 A; A=1-417.
PDB; 3K3Q; X-ray; 2.60 A; B=3-250, C=251-425.
PDB; 3QIX; X-ray; 2.41 A; A/B=3-424.
PDB; 3QIY; X-ray; 2.30 A; A=3-424.
PDB; 3QIZ; X-ray; 2.00 A; A=3-424.
PDB; 3QJ0; X-ray; 2.30 A; A=3-424.
PDB; 3QW5; X-ray; 1.60 A; A=1-424.
PDB; 3QW6; X-ray; 1.60 A; A=1-424.
PDB; 3QW7; X-ray; 1.50 A; A=1-424.
PDB; 3QW8; X-ray; 1.60 A; A=1-424.
PDB; 4KS6; X-ray; 1.93 A; A=1-425.
PDB; 4KTX; X-ray; 2.59 A; A=1-425.
PDB; 4KUF; X-ray; 1.70 A; A=1-425.
PDB; 5L21; X-ray; 1.68 A; A=872-1296.
PDBsum; 1XTF; -.
PDBsum; 1XTG; -.
PDBsum; 2W2D; -.
PDBsum; 3DSE; -.
PDBsum; 3K3Q; -.
PDBsum; 3QIX; -.
PDBsum; 3QIY; -.
PDBsum; 3QIZ; -.
PDBsum; 3QJ0; -.
PDBsum; 3QW5; -.
PDBsum; 3QW6; -.
PDBsum; 3QW7; -.
PDBsum; 3QW8; -.
PDBsum; 4KS6; -.
PDBsum; 4KTX; -.
PDBsum; 4KUF; -.
PDBsum; 5L21; -.
ProteinModelPortal; A5HZZ9; -.
SMR; A5HZZ9; -.
DIP; DIP-61682N; -.
IntAct; A5HZZ9; 1.
BindingDB; A5HZZ9; -.
ChEMBL; CHEMBL5344; -.
EnsemblBacteria; ABS38337; ABS38337; CLC_0862.
GeneID; 5185061; -.
GeneID; 5398487; -.
KEGG; cbh:CLC_0862; -.
KEGG; cbo:CBO0806; -.
PATRIC; fig|413999.7.peg.802; -.
HOGENOM; HOG000234384; -.
KO; K06011; -.
OMA; DEGYNKA; -.
BioCyc; CBOT441771:G1G97-810-MONOMER; -.
EvolutionaryTrace; A5HZZ9; -.
PRO; PR:A5HZZ9; -.
Proteomes; UP000001986; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
GO; GO:0044156; C:host cell junction; IEA:UniProtKB-KW.
GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; -; 1.
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; Complete proteome; Direct protein sequencing;
Disulfide bond; Host cell junction; Host cell membrane;
Host cytoplasm; Host membrane; Host synapse; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Neurotoxin; Pharmaceutical; Protease;
Reference proteome; Secreted; Toxin; Transmembrane;
Transmembrane helix; Virulence; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 448 Botulinum neurotoxin A light chain.
/FTId=PRO_0000308906.
CHAIN 449 1296 Botulinum neurotoxin A heavy chain.
/FTId=PRO_0000308907.
TRANSMEM 627 647 Helical. {ECO:0000255}.
TRANSMEM 656 676 Helical. {ECO:0000255}.
ACT_SITE 224 224 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 223 223 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 227 227 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 262 262 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
DISULFID 430 454 Interchain (between light and heavy
chains). {ECO:0000250}.
DISULFID 1235 1280 {ECO:0000250}.
CONFLICT 1218 1218 S -> Y (in Ref. 4; AA sequence).
{ECO:0000305}.
STRAND 4 6 {ECO:0000244|PDB:3QW7}.
STRAND 16 23 {ECO:0000244|PDB:3QW7}.
STRAND 26 28 {ECO:0000244|PDB:3QW6}.
STRAND 33 39 {ECO:0000244|PDB:3QW7}.
STRAND 42 48 {ECO:0000244|PDB:3QW7}.
STRAND 50 52 {ECO:0000244|PDB:4KUF}.
HELIX 54 56 {ECO:0000244|PDB:3QW7}.
STRAND 63 65 {ECO:0000244|PDB:3QW7}.
TURN 68 70 {ECO:0000244|PDB:3DSE}.
TURN 75 78 {ECO:0000244|PDB:3QW7}.
HELIX 81 99 {ECO:0000244|PDB:3QW7}.
HELIX 102 113 {ECO:0000244|PDB:3QW7}.
STRAND 126 128 {ECO:0000244|PDB:3QW7}.
HELIX 131 133 {ECO:0000244|PDB:3QW7}.
STRAND 134 138 {ECO:0000244|PDB:3QW7}.
STRAND 144 148 {ECO:0000244|PDB:3QW7}.
STRAND 150 155 {ECO:0000244|PDB:3QW7}.
STRAND 164 166 {ECO:0000244|PDB:3QW7}.
STRAND 169 171 {ECO:0000244|PDB:4KTX}.
TURN 175 177 {ECO:0000244|PDB:3QW7}.
STRAND 184 187 {ECO:0000244|PDB:3QW7}.
STRAND 192 196 {ECO:0000244|PDB:3QW7}.
HELIX 200 203 {ECO:0000244|PDB:3QW7}.
STRAND 211 214 {ECO:0000244|PDB:3DSE}.
HELIX 217 232 {ECO:0000244|PDB:3QW7}.
STRAND 242 244 {ECO:0000244|PDB:3QW7}.
HELIX 249 252 {ECO:0000244|PDB:3QW7}.
TURN 253 255 {ECO:0000244|PDB:3QW7}.
STRAND 257 259 {ECO:0000244|PDB:3QW7}.
HELIX 260 266 {ECO:0000244|PDB:3QW7}.
HELIX 268 273 {ECO:0000244|PDB:3QW7}.
HELIX 276 299 {ECO:0000244|PDB:3QW7}.
STRAND 302 308 {ECO:0000244|PDB:3QW7}.
HELIX 310 321 {ECO:0000244|PDB:3QW7}.
STRAND 323 325 {ECO:0000244|PDB:3QIX}.
STRAND 327 329 {ECO:0000244|PDB:3QW5}.
STRAND 331 333 {ECO:0000244|PDB:3QIX}.
HELIX 335 347 {ECO:0000244|PDB:3QW7}.
HELIX 351 358 {ECO:0000244|PDB:3QW7}.
STRAND 366 368 {ECO:0000244|PDB:3QW7}.
STRAND 372 375 {ECO:0000244|PDB:3QW7}.
TURN 381 383 {ECO:0000244|PDB:3QW7}.
TURN 386 388 {ECO:0000244|PDB:3QW7}.
STRAND 393 395 {ECO:0000244|PDB:2W2D}.
HELIX 396 398 {ECO:0000244|PDB:3QJ0}.
TURN 400 404 {ECO:0000244|PDB:3QW7}.
TURN 406 409 {ECO:0000244|PDB:3QW7}.
HELIX 410 412 {ECO:0000244|PDB:3QW7}.
STRAND 414 418 {ECO:0000244|PDB:3QW7}.
TURN 420 422 {ECO:0000244|PDB:3QW8}.
STRAND 425 431 {ECO:0000244|PDB:2W2D}.
STRAND 453 458 {ECO:0000244|PDB:2W2D}.
HELIX 459 461 {ECO:0000244|PDB:2W2D}.
HELIX 468 470 {ECO:0000244|PDB:2W2D}.
STRAND 479 481 {ECO:0000244|PDB:2W2D}.
HELIX 496 504 {ECO:0000244|PDB:2W2D}.
STRAND 542 547 {ECO:0000244|PDB:2W2D}.
HELIX 550 556 {ECO:0000244|PDB:2W2D}.
STRAND 568 572 {ECO:0000244|PDB:2W2D}.
HELIX 573 575 {ECO:0000244|PDB:2W2D}.
STRAND 581 583 {ECO:0000244|PDB:2W2D}.
HELIX 588 595 {ECO:0000244|PDB:2W2D}.
TURN 600 602 {ECO:0000244|PDB:2W2D}.
HELIX 603 618 {ECO:0000244|PDB:2W2D}.
STRAND 625 629 {ECO:0000244|PDB:2W2D}.
HELIX 637 641 {ECO:0000244|PDB:2W2D}.
TURN 642 644 {ECO:0000244|PDB:2W2D}.
HELIX 649 659 {ECO:0000244|PDB:2W2D}.
HELIX 660 663 {ECO:0000244|PDB:2W2D}.
STRAND 679 681 {ECO:0000244|PDB:2W2D}.
HELIX 688 720 {ECO:0000244|PDB:2W2D}.
HELIX 722 752 {ECO:0000244|PDB:2W2D}.
HELIX 758 762 {ECO:0000244|PDB:2W2D}.
HELIX 766 799 {ECO:0000244|PDB:2W2D}.
HELIX 801 825 {ECO:0000244|PDB:2W2D}.
TURN 826 829 {ECO:0000244|PDB:2W2D}.
HELIX 834 845 {ECO:0000244|PDB:2W2D}.
HELIX 853 855 {ECO:0000244|PDB:2W2D}.
HELIX 860 870 {ECO:0000244|PDB:2W2D}.
HELIX 872 875 {ECO:0000244|PDB:5L21}.
STRAND 878 884 {ECO:0000244|PDB:5L21}.
STRAND 887 890 {ECO:0000244|PDB:5L21}.
STRAND 897 900 {ECO:0000244|PDB:5L21}.
STRAND 914 919 {ECO:0000244|PDB:5L21}.
STRAND 924 927 {ECO:0000244|PDB:5L21}.
HELIX 930 932 {ECO:0000244|PDB:5L21}.
STRAND 935 938 {ECO:0000244|PDB:5L21}.
STRAND 941 948 {ECO:0000244|PDB:5L21}.
HELIX 955 957 {ECO:0000244|PDB:5L21}.
STRAND 962 969 {ECO:0000244|PDB:5L21}.
STRAND 972 979 {ECO:0000244|PDB:5L21}.
STRAND 982 988 {ECO:0000244|PDB:5L21}.
STRAND 994 1000 {ECO:0000244|PDB:5L21}.
STRAND 1003 1007 {ECO:0000244|PDB:5L21}.
STRAND 1015 1021 {ECO:0000244|PDB:5L21}.
STRAND 1025 1031 {ECO:0000244|PDB:5L21}.
STRAND 1034 1040 {ECO:0000244|PDB:5L21}.
STRAND 1051 1059 {ECO:0000244|PDB:5L21}.
STRAND 1066 1077 {ECO:0000244|PDB:5L21}.
HELIX 1081 1091 {ECO:0000244|PDB:5L21}.
STRAND 1102 1104 {ECO:0000244|PDB:5L21}.
STRAND 1110 1118 {ECO:0000244|PDB:5L21}.
STRAND 1122 1129 {ECO:0000244|PDB:5L21}.
STRAND 1134 1138 {ECO:0000244|PDB:5L21}.
STRAND 1142 1145 {ECO:0000244|PDB:5L21}.
TURN 1146 1148 {ECO:0000244|PDB:5L21}.
STRAND 1149 1152 {ECO:0000244|PDB:5L21}.
STRAND 1160 1164 {ECO:0000244|PDB:5L21}.
STRAND 1179 1186 {ECO:0000244|PDB:5L21}.
STRAND 1189 1195 {ECO:0000244|PDB:5L21}.
STRAND 1202 1205 {ECO:0000244|PDB:5L21}.
STRAND 1207 1209 {ECO:0000244|PDB:5L21}.
HELIX 1211 1213 {ECO:0000244|PDB:5L21}.
STRAND 1220 1223 {ECO:0000244|PDB:5L21}.
STRAND 1237 1240 {ECO:0000244|PDB:5L21}.
STRAND 1246 1255 {ECO:0000244|PDB:5L21}.
STRAND 1258 1264 {ECO:0000244|PDB:5L21}.
HELIX 1266 1273 {ECO:0000244|PDB:5L21}.
STRAND 1281 1285 {ECO:0000244|PDB:5L21}.
SEQUENCE 1296 AA; 149426 MW; DEA8CF2754AE43E6 CRC64;
MPFVNKQFNY KDPVNGVDIA YIKIPNAGQM QPVKAFKIHN KIWVIPERDT FTNPEEGDLN
PPPEAKQVPV SYYDSTYLST DNEKDNYLKG VTKLFERIYS TDLGRMLLTS IVRGIPFWGG
STIDTELKVI DTNCINVIQP DGSYRSEELN LVIIGPSADI IQFECKSFGH EVLNLTRNGY
GSTQYIRFSP DFTFGFEESL EVDTNPLLGA GKFATDPAVT LAHELIHAGH RLYGIAINPN
RVFKVNTNAY YEMSGLEVSF EELRTFGGHD AKFIDSLQEN EFRLYYYNKF KDIASTLNKA
KSIVGTTASL QYMKNVFKEK YLLSEDTSGK FSVDKLKFDK LYKMLTEIYT EDNFVKFFKV
LNRKTYLNFD KAVFKINIVP KVNYTIYDGF NLRNTNLAAN FNGQNTEINN MNFTKLKNFT
GLFEFYKLLC VRGIITSKTK SLDKGYNKAL NDLCIKVNNW DLFFSPSEDN FTNDLNKGEE
ITSDTNIEAA EENISLDLIQ QYYLTFNFDN EPENISIENL SSDIIGQLEL MPNIERFPNG
KKYELDKYTM FHYLRAQEFE HGKSRIALTN SVNEALLNPS RVYTFFSSDY VKKVNKATEA
AMFLGWVEQL VYDFTDETSE VSTTDKIADI TIIIPYIGPA LNIGNMLYKD DFVGALIFSG
AVILLEFIPE IAIPVLGTFA LVSYIANKVL TVQTIDNALS KRNEKWDEVY KYIVTNWLAK
VNTQIDLIRK KMKEALENQA EATKAIINYQ YNQYTEEEKN NINFNIDDLS SKLNESINKA
MININKFLNQ CSVSYLMNSM IPYGVKRLED FDASLKDALL KYIYDNRGTL IGQVDRLKDK
VNNTLSTDIP FQLSKYVDNQ RLLSTFTEYI KNIINTSILN LRYESNHLID LSRYASKINI
GSKVNFDPID KNQIQLFNLE SSKIEVILKN AIVYNSMYEN FSTSFWIRIP KYFNSISLNN
EYTIINCMEN NSGWKVSLNY GEIIWTLQDT QEIKQRVVFK YSQMINISDY INRWIFVTIT
NNRLNNSKIY INGRLIDQKP ISNLGNIHAS NNIMFKLDGC RDTHRYIWIK YFNLFDKELN
EKEIKDLYDN QSNSGILKDF WGDYLQYDKP YYMLNLYDPN KYVDVNNVGI RGYMYLKGPR
GSVMTTNIYL NSSLYRGTKF IIKKYASGNK DNIVRNNDRV YINVVVKNKE YRLATNASQA
GVEKILSALE IPDVGNLSQV VVMKSKNDQG ITNKCKMNLQ DNNGNDIGFI GFHQFNNIAK
LVASNWYNRQ IERSSRTLGC SWEFIPVDDG WGERPL


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