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

 BXB_CLOBO               Reviewed;        1291 AA.
P10844; P10843;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-DEC-2017, entry version 159.
RecName: Full=Botulinum neurotoxin type B;
Short=BoNT/B;
EC=3.4.24.69;
AltName: Full=Bontoxilysin-B;
Contains:
RecName: Full=Botulinum neurotoxin B light chain;
Contains:
RecName: Full=Botulinum neurotoxin B heavy chain;
Flags: Precursor;
Name=botB;
Clostridium botulinum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1491;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1514783;
Whelan S.M., Elmore M.J., Bodsworth N.J., Brehm J.K., Atkinson T.,
Minton N.P.;
"Molecular cloning of the Clostridium botulinum structural gene
encoding the type B neurotoxin and determination of its entire
nucleotide sequence.";
Appl. Environ. Microbiol. 58:2345-2354(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-246.
STRAIN=Type B / NCTC 7273;
Szabo E.A., Pemberton J.M., Desmarchelier P.M.;
Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-994.
STRAIN=Type B / NCTC 7273;
PubMed=8408542;
Campbell K.D., Collins M.D., East A.K.;
"Gene probes for identification of the botulinal neurotoxin gene and
specific identification of neurotoxin types B, E, and F.";
J. Clin. Microbiol. 31:2255-2262(1993).
[4]
PROTEIN SEQUENCE OF 2-45 AND 442-467.
STRAIN=Type B / B-657;
PubMed=3139097; DOI=10.1016/0300-9084(88)90111-3;
Dasgupta B.R., Datta A.;
"Botulinum neurotoxin type B (strain 657): partial sequence and
similarity with tetanus toxin.";
Biochimie 70:811-817(1988).
[5]
IDENTIFICATION AS A ZINC-PROTEASE.
PubMed=1429690;
Schiavo G., Rossetto O., Santucci A., Dasgupta B.R., Montecucco C.;
"Botulinum neurotoxins are zinc proteins.";
J. Biol. Chem. 267:23479-23483(1992).
[6]
IDENTIFICATION OF SUBSTRATE.
PubMed=1331807; DOI=10.1038/359832a0;
Schiavo G., Benfenati F., Poulain B., Rossetto O., de Laureto P.P.,
Dasgupta B.R., Montecucco C.;
"Tetanus and botulinum-B neurotoxins block neurotransmitter release by
proteolytic cleavage of synaptobrevin.";
Nature 359:832-835(1992).
-!- 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 that cleaves the '76-Gln-|-Phe-77' bond of
synaptobrevin-2.
-!- 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.
-!- INTERACTION:
P29101:Syt2 (xeno); NbExp=6; IntAct=EBI-7661991, EBI-458017;
P46097:Syt2 (xeno); NbExp=3; IntAct=EBI-7661991, EBI-457969;
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin B light chain:
Secreted. Host cytoplasm, host cytosol.
-!- SUBCELLULAR LOCATION: Botulinum neurotoxin B heavy chain:
Secreted. Host cell junction, host synapse, host presynaptic cell
membrane {ECO:0000305}.
-!- 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; M81186; AAA23211.1; -; Genomic_DNA.
EMBL; Z11934; CAA77991.1; -; Genomic_DNA.
EMBL; X70817; CAA50148.1; -; Genomic_DNA.
PIR; A48940; A48940.
PDB; 1EPW; X-ray; 1.90 A; A=2-1291.
PDB; 1F31; X-ray; 2.60 A; A=2-1291.
PDB; 1F82; X-ray; 2.20 A; A=2-425.
PDB; 1G9A; X-ray; 2.10 A; A=2-1291.
PDB; 1G9B; X-ray; 2.00 A; A=2-1291.
PDB; 1G9C; X-ray; 2.35 A; A=2-1291.
PDB; 1G9D; X-ray; 2.20 A; A=2-1291.
PDB; 1I1E; X-ray; 2.50 A; A=2-1291.
PDB; 1S0B; X-ray; 2.00 A; A=2-1291.
PDB; 1S0C; X-ray; 2.20 A; A=2-1291.
PDB; 1S0D; X-ray; 2.20 A; A=2-1291.
PDB; 1S0E; X-ray; 1.90 A; A=2-1291.
PDB; 1S0F; X-ray; 2.30 A; A=2-1291.
PDB; 1S0G; X-ray; 2.60 A; A=2-1291.
PDB; 1Z0H; X-ray; 2.00 A; A/B=854-1291.
PDB; 2ETF; X-ray; 2.29 A; A/B=1-441.
PDB; 2NM1; X-ray; 2.15 A; A=858-1291.
PDB; 2NP0; X-ray; 2.62 A; A=2-1291.
PDB; 2XHL; X-ray; 2.80 A; A=1-437, B=446-858.
PDB; 3ZUQ; X-ray; 2.70 A; A=1-437, A=446-858.
PDB; 4KBB; X-ray; 2.30 A; A/B=857-1291.
PDB; 5VID; X-ray; 2.75 A; A/B/C/D/E=859-1291.
PDB; 5VMR; X-ray; 1.95 A; A/B=859-1291.
PDBsum; 1EPW; -.
PDBsum; 1F31; -.
PDBsum; 1F82; -.
PDBsum; 1G9A; -.
PDBsum; 1G9B; -.
PDBsum; 1G9C; -.
PDBsum; 1G9D; -.
PDBsum; 1I1E; -.
PDBsum; 1S0B; -.
PDBsum; 1S0C; -.
PDBsum; 1S0D; -.
PDBsum; 1S0E; -.
PDBsum; 1S0F; -.
PDBsum; 1S0G; -.
PDBsum; 1Z0H; -.
PDBsum; 2ETF; -.
PDBsum; 2NM1; -.
PDBsum; 2NP0; -.
PDBsum; 2XHL; -.
PDBsum; 3ZUQ; -.
PDBsum; 4KBB; -.
PDBsum; 5VID; -.
PDBsum; 5VMR; -.
ProteinModelPortal; P10844; -.
SMR; P10844; -.
DIP; DIP-42782N; -.
IntAct; P10844; 4.
MINT; MINT-1795550; -.
BindingDB; P10844; -.
ChEMBL; CHEMBL1075064; -.
DrugBank; DB02379; Beta-D-Glucose.
DrugBank; DB01705; Bis(5-Amidino-Benzimidazolyl)Methane.
DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
MEROPS; M27.002; -.
BRENDA; 3.4.24.69; 1462.
Reactome; R-HSA-5250958; Toxicity of botulinum toxin type B (BoNT/B).
EvolutionaryTrace; P10844; -.
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; EXP:Reactome.
GO; GO:0008320; F:protein transmembrane transporter activity; EXP: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.
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; Direct protein sequencing; Disulfide bond;
Host cell junction; Host cell membrane; Host cytoplasm; Host membrane;
Host synapse; Hydrolase; Membrane; Metal-binding; Metalloprotease;
Neurotoxin; Protease; Secreted; Toxin; Transmembrane; Virulence; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3139097}.
CHAIN 2 441 Botulinum neurotoxin B light chain.
/FTId=PRO_0000029215.
CHAIN 442 1291 Botulinum neurotoxin B heavy chain.
/FTId=PRO_0000029216.
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 437 446 Interchain (between light and heavy
chains). {ECO:0000305}.
CONFLICT 30 30 T -> M (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 218 218 R -> G (in Ref. 2; CAA77991).
{ECO:0000305}.
CONFLICT 225 225 A -> S (in Ref. 2; CAA77991).
{ECO:0000305}.
CONFLICT 464 464 S -> R (in Ref. 4; AA sequence).
{ECO:0000305}.
STRAND 16 23 {ECO:0000244|PDB:1EPW}.
HELIX 25 27 {ECO:0000244|PDB:1EPW}.
TURN 28 31 {ECO:0000244|PDB:1F82}.
STRAND 34 40 {ECO:0000244|PDB:1EPW}.
STRAND 43 46 {ECO:0000244|PDB:1EPW}.
HELIX 56 59 {ECO:0000244|PDB:1EPW}.
STRAND 63 66 {ECO:0000244|PDB:1EPW}.
STRAND 72 74 {ECO:0000244|PDB:1EPW}.
TURN 76 79 {ECO:0000244|PDB:1EPW}.
HELIX 82 99 {ECO:0000244|PDB:1EPW}.
HELIX 103 114 {ECO:0000244|PDB:1EPW}.
STRAND 122 124 {ECO:0000244|PDB:1G9D}.
TURN 134 136 {ECO:0000244|PDB:1EPW}.
STRAND 137 141 {ECO:0000244|PDB:1EPW}.
STRAND 145 148 {ECO:0000244|PDB:1F82}.
STRAND 151 155 {ECO:0000244|PDB:1EPW}.
STRAND 157 161 {ECO:0000244|PDB:1EPW}.
STRAND 171 173 {ECO:0000244|PDB:1EPW}.
STRAND 176 179 {ECO:0000244|PDB:1G9D}.
HELIX 182 184 {ECO:0000244|PDB:1EPW}.
STRAND 185 187 {ECO:0000244|PDB:1EPW}.
STRAND 191 194 {ECO:0000244|PDB:1EPW}.
STRAND 197 203 {ECO:0000244|PDB:1EPW}.
STRAND 206 208 {ECO:0000244|PDB:1G9B}.
STRAND 210 212 {ECO:0000244|PDB:1S0E}.
STRAND 214 216 {ECO:0000244|PDB:1EPW}.
STRAND 219 221 {ECO:0000244|PDB:1EPW}.
HELIX 224 239 {ECO:0000244|PDB:1EPW}.
HELIX 266 272 {ECO:0000244|PDB:1EPW}.
HELIX 276 279 {ECO:0000244|PDB:1EPW}.
HELIX 282 305 {ECO:0000244|PDB:1EPW}.
STRAND 308 311 {ECO:0000244|PDB:1EPW}.
HELIX 317 327 {ECO:0000244|PDB:1EPW}.
STRAND 330 332 {ECO:0000244|PDB:1F82}.
STRAND 338 340 {ECO:0000244|PDB:1F82}.
HELIX 342 354 {ECO:0000244|PDB:1EPW}.
HELIX 358 365 {ECO:0000244|PDB:1EPW}.
STRAND 373 375 {ECO:0000244|PDB:1EPW}.
STRAND 378 384 {ECO:0000244|PDB:1EPW}.
TURN 389 391 {ECO:0000244|PDB:1EPW}.
TURN 394 396 {ECO:0000244|PDB:1EPW}.
HELIX 401 403 {ECO:0000244|PDB:1EPW}.
HELIX 407 412 {ECO:0000244|PDB:1EPW}.
TURN 414 416 {ECO:0000244|PDB:1EPW}.
HELIX 418 420 {ECO:0000244|PDB:1EPW}.
STRAND 421 423 {ECO:0000244|PDB:1S0E}.
HELIX 426 428 {ECO:0000244|PDB:1EPW}.
STRAND 433 437 {ECO:0000244|PDB:1EPW}.
STRAND 446 450 {ECO:0000244|PDB:1EPW}.
HELIX 451 453 {ECO:0000244|PDB:1EPW}.
HELIX 460 462 {ECO:0000244|PDB:1EPW}.
HELIX 466 468 {ECO:0000244|PDB:1EPW}.
STRAND 471 473 {ECO:0000244|PDB:1EPW}.
HELIX 488 493 {ECO:0000244|PDB:1EPW}.
STRAND 495 498 {ECO:0000244|PDB:1EPW}.
STRAND 506 508 {ECO:0000244|PDB:1EPW}.
STRAND 524 531 {ECO:0000244|PDB:1EPW}.
HELIX 537 542 {ECO:0000244|PDB:1EPW}.
STRAND 554 557 {ECO:0000244|PDB:1EPW}.
HELIX 559 564 {ECO:0000244|PDB:1EPW}.
STRAND 568 570 {ECO:0000244|PDB:1EPW}.
HELIX 575 581 {ECO:0000244|PDB:1EPW}.
HELIX 587 606 {ECO:0000244|PDB:1EPW}.
HELIX 607 609 {ECO:0000244|PDB:1EPW}.
STRAND 610 612 {ECO:0000244|PDB:1G9B}.
HELIX 613 615 {ECO:0000244|PDB:1EPW}.
STRAND 617 620 {ECO:0000244|PDB:1G9B}.
HELIX 624 628 {ECO:0000244|PDB:1EPW}.
TURN 631 635 {ECO:0000244|PDB:1EPW}.
HELIX 639 646 {ECO:0000244|PDB:1EPW}.
HELIX 647 651 {ECO:0000244|PDB:1EPW}.
STRAND 666 668 {ECO:0000244|PDB:1EPW}.
HELIX 675 707 {ECO:0000244|PDB:1EPW}.
HELIX 709 738 {ECO:0000244|PDB:1EPW}.
HELIX 743 747 {ECO:0000244|PDB:1EPW}.
HELIX 753 786 {ECO:0000244|PDB:1EPW}.
HELIX 788 812 {ECO:0000244|PDB:1EPW}.
HELIX 814 817 {ECO:0000244|PDB:1EPW}.
TURN 819 824 {ECO:0000244|PDB:1EPW}.
HELIX 825 831 {ECO:0000244|PDB:1EPW}.
HELIX 840 842 {ECO:0000244|PDB:1EPW}.
HELIX 847 857 {ECO:0000244|PDB:1EPW}.
HELIX 860 863 {ECO:0000244|PDB:1EPW}.
STRAND 864 870 {ECO:0000244|PDB:1EPW}.
STRAND 872 877 {ECO:0000244|PDB:1EPW}.
STRAND 879 881 {ECO:0000244|PDB:1EPW}.
STRAND 884 887 {ECO:0000244|PDB:1EPW}.
STRAND 891 893 {ECO:0000244|PDB:5VMR}.
STRAND 897 901 {ECO:0000244|PDB:1EPW}.
STRAND 909 912 {ECO:0000244|PDB:1EPW}.
TURN 915 917 {ECO:0000244|PDB:2NP0}.
STRAND 918 923 {ECO:0000244|PDB:5VMR}.
STRAND 926 933 {ECO:0000244|PDB:1EPW}.
HELIX 939 941 {ECO:0000244|PDB:1EPW}.
HELIX 942 947 {ECO:0000244|PDB:1EPW}.
STRAND 949 957 {ECO:0000244|PDB:1EPW}.
STRAND 960 967 {ECO:0000244|PDB:1EPW}.
STRAND 970 976 {ECO:0000244|PDB:1EPW}.
STRAND 978 980 {ECO:0000244|PDB:1S0F}.
STRAND 982 988 {ECO:0000244|PDB:1EPW}.
STRAND 991 995 {ECO:0000244|PDB:2NM1}.
STRAND 1003 1009 {ECO:0000244|PDB:1EPW}.
STRAND 1011 1018 {ECO:0000244|PDB:1EPW}.
STRAND 1021 1027 {ECO:0000244|PDB:1EPW}.
STRAND 1038 1047 {ECO:0000244|PDB:1EPW}.
STRAND 1054 1064 {ECO:0000244|PDB:1EPW}.
HELIX 1068 1079 {ECO:0000244|PDB:1EPW}.
STRAND 1089 1091 {ECO:0000244|PDB:1EPW}.
STRAND 1093 1095 {ECO:0000244|PDB:1Z0H}.
STRAND 1097 1102 {ECO:0000244|PDB:1EPW}.
HELIX 1103 1105 {ECO:0000244|PDB:1Z0H}.
STRAND 1108 1112 {ECO:0000244|PDB:1EPW}.
STRAND 1116 1123 {ECO:0000244|PDB:1EPW}.
STRAND 1145 1149 {ECO:0000244|PDB:1EPW}.
TURN 1153 1155 {ECO:0000244|PDB:1S0G}.
STRAND 1166 1173 {ECO:0000244|PDB:1EPW}.
STRAND 1176 1183 {ECO:0000244|PDB:1EPW}.
STRAND 1188 1192 {ECO:0000244|PDB:1EPW}.
STRAND 1194 1198 {ECO:0000244|PDB:1EPW}.
STRAND 1202 1205 {ECO:0000244|PDB:5VMR}.
STRAND 1208 1211 {ECO:0000244|PDB:1EPW}.
STRAND 1215 1217 {ECO:0000244|PDB:5VID}.
STRAND 1221 1231 {ECO:0000244|PDB:1EPW}.
STRAND 1234 1246 {ECO:0000244|PDB:1EPW}.
STRAND 1248 1250 {ECO:0000244|PDB:2NM1}.
STRAND 1251 1260 {ECO:0000244|PDB:1EPW}.
HELIX 1263 1266 {ECO:0000244|PDB:1EPW}.
STRAND 1269 1271 {ECO:0000244|PDB:1EPW}.
STRAND 1280 1283 {ECO:0000244|PDB:1EPW}.
SEQUENCE 1291 AA; 150803 MW; 921DE5C518140DBD CRC64;
MPVTINNFNY NDPIDNNNII MMEPPFARGT GRYYKAFKIT DRIWIIPERY TFGYKPEDFN
KSSGIFNRDV CEYYDPDYLN TNDKKNIFLQ TMIKLFNRIK SKPLGEKLLE MIINGIPYLG
DRRVPLEEFN TNIASVTVNK LISNPGEVER KKGIFANLII FGPGPVLNEN ETIDIGIQNH
FASREGFGGI MQMKFCPEYV SVFNNVQENK GASIFNRRGY FSDPALILMH ELIHVLHGLY
GIKVDDLPIV PNEKKFFMQS TDAIQAEELY TFGGQDPSII TPSTDKSIYD KVLQNFRGIV
DRLNKVLVCI SDPNININIY KNKFKDKYKF VEDSEGKYSI DVESFDKLYK SLMFGFTETN
IAENYKIKTR ASYFSDSLPP VKIKNLLDNE IYTIEEGFNI SDKDMEKEYR GQNKAINKQA
YEEISKEHLA VYKIQMCKSV KAPGICIDVD NEDLFFIADK NSFSDDLSKN ERIEYNTQSN
YIENDFPINE LILDTDLISK IELPSENTES LTDFNVDVPV YEKQPAIKKI FTDENTIFQY
LYSQTFPLDI RDISLTSSFD DALLFSNKVY SFFSMDYIKT ANKVVEAGLF AGWVKQIVND
FVIEANKSNT MDKIADISLI VPYIGLALNV GNETAKGNFE NAFEIAGASI LLEFIPELLI
PVVGAFLLES YIDNKNKIIK TIDNALTKRN EKWSDMYGLI VAQWLSTVNT QFYTIKEGMY
KALNYQAQAL EEIIKYRYNI YSEKEKSNIN IDFNDINSKL NEGINQAIDN INNFINGCSV
SYLMKKMIPL AVEKLLDFDN TLKKNLLNYI DENKLYLIGS AEYEKSKVNK YLKTIMPFDL
SIYTNDTILI EMFNKYNSEI LNNIILNLRY KDNNLIDLSG YGAKVEVYDG VELNDKNQFK
LTSSANSKIR VTQNQNIIFN SVFLDFSVSF WIRIPKYKND GIQNYIHNEY TIINCMKNNS
GWKISIRGNR IIWTLIDING KTKSVFFEYN IREDISEYIN RWFFVTITNN LNNAKIYING
KLESNTDIKD IREVIANGEI IFKLDGDIDR TQFIWMKYFS IFNTELSQSN IEERYKIQSY
SEYLKDFWGN PLMYNKEYYM FNAGNKNSYI KLKKDSPVGE ILTRSKYNQN SKYINYRDLY
IGEKFIIRRK SNSQSINDDI VRKEDYIYLD FFNLNQEWRV YTYKYFKKEE EKLFLAPISD
SDEFYNTIQI KEYDEQPTYS CQLLFKKDEE STDEIGLIGI HRFYESGIVF EEYKDYFCIS
KWYLKEVKRK PYNLKLGCNW QFIPKDEGWT E


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