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1.C.8.1.1
Botulinum neurotoxin types A-G.  Poly(amindo)amine (PAMAM) detrimers block activity (Förstner et al. 2014).  BoNTs inhibit synaptic exocytosis; intoxication requires the di-chain protein to undergo conformational changes in response to pH and redox gradients across the endosomal membrane with consequent formation of a protein-conducting channel by the heavy chain (HC) that translocates the light chain (LC) protease into the cytosol, colocalizing it with the substrate SNARE proteins (Montal 2009).

Accession Number:P10845
Protein Name:BXA aka BOTA aka BNA aka ATX
Length:1296
Molecular Weight:149454.00
Species:Clostridium botulinum [1491]
Location1 / Topology2 / Orientation3: Secreted1 / Multi-pass membrane protein2
Substrate peptides

Cross database links:

Pfam: PF01742    PF07951    PF07953    PF07952   

Gene Ontology

GO:0005829 C:cytosol
GO:0030666 C:endocytic vesicle membrane
GO:0044164 C:host cell cytosol
GO:0044156 C:host cell junction
GO:0044231 C:host cell presynaptic membrane
GO:0016021 C:integral to membrane
GO:0004222 F:metalloendopeptidase activity
GO:0050827 F:toxin receptor binding
GO:0008270 F:zinc ion binding
GO:0051609 P:inhibition of neurotransmitter uptake
GO:0009405 P:pathogenesis
GO:0006508 P:proteolysis

References (12)

[1] “The complete amino acid sequence of the Clostridium botulinum type A neurotoxin, deduced by nucleotide sequence analysis of the encoding gene.”  Thompson D.E.et.al.   2185020
[2] “The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins.”  Binz T.et.al.   2160960
[3] “Organization and phylogenetic interrelationships of genes encoding components of the botulinum toxin complex in proteolytic Clostridium botulinum types A, B, and F: evidence of chimeric sequences in the gene encoding the nontoxic nonhemagglutinin component.”  East A.K.et.al.   8863443
[4] “Molecular characterization of two forms of nontoxic-nonhemagglutinin components of Clostridium botulinum type A progenitor toxins.”  Fujita R.et.al.   8521962
[5] “Partial amino acid sequence of the heavy and light chains of botulinum neurotoxin type A.”  Schmidt J.J.et.al.   6370252
[6] “Botulinum neurotoxin type A: sequence of amino acids at the N-terminus and around the nicking site.”  Dasgupta B.R.et.al.   2126206
[7] “Botulinum neurotoxin type A: cleavage of the heavy chain into two halves and their partial sequences.”  Sathymoorthy V.et.al.   3178218
[8] “Inactivation of Clostridium botulinum type A neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity.”  Shone C.C.et.al.   3896784
[9] “Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds.”  Schiavo G.et.al.   8243676
[10] “Site-directed mutagenesis identifies active-site residues of the light chain of botulinum neurotoxin type a.”  Rigoni M.et.al.   11700044
[11] “SV2 is the protein receptor for botulinum neurotoxin A.”  Dong M.et.al.   16543415
[12] “Crystal structure of botulinum neurotoxin type A and implications for toxicity.”  Lacy D.B.et.al.   9783750
Structure:
1UEE   1XTF   1XTG   2ILP   2IMA   2IMB   2IMC   2ISE   2ISG   2ISH   [...more]

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MPFVNKQFNY KDPVNGVDIA YIKIPNVGQM QPVKAFKIHN KIWVIPERDT FTNPEEGDLN 
61:	PPPEAKQVPV SYYDSTYLST DNEKDNYLKG VTKLFERIYS TDLGRMLLTS IVRGIPFWGG 
121:	STIDTELKVI DTNCINVIQP DGSYRSEELN LVIIGPSADI IQFECKSFGH EVLNLTRNGY 
181:	GSTQYIRFSP DFTFGFEESL EVDTNPLLGA GKFATDPAVT LAHELIHAGH RLYGIAINPN 
241:	RVFKVNTNAY YEMSGLEVSF EELRTFGGHD AKFIDSLQEN EFRLYYYNKF KDIASTLNKA 
301:	KSIVGTTASL QYMKNVFKEK YLLSEDTSGK FSVDKLKFDK LYKMLTEIYT EDNFVKFFKV 
361:	LNRKTYLNFD KAVFKINIVP KVNYTIYDGF NLRNTNLAAN FNGQNTEINN MNFTKLKNFT 
421:	GLFEFYKLLC VRGIITSKTK SLDKGYNKAL NDLCIKVNNW DLFFSPSEDN FTNDLNKGEE 
481:	ITSDTNIEAA EENISLDLIQ QYYLTFNFDN EPENISIENL SSDIIGQLEL MPNIERFPNG 
541:	KKYELDKYTM FHYLRAQEFE HGKSRIALTN SVNEALLNPS RVYTFFSSDY VKKVNKATEA 
601:	AMFLGWVEQL VYDFTDETSE VSTTDKIADI TIIIPYIGPA LNIGNMLYKD DFVGALIFSG 
661:	AVILLEFIPE IAIPVLGTFA LVSYIANKVL TVQTIDNALS KRNEKWDEVY KYIVTNWLAK 
721:	VNTQIDLIRK KMKEALENQA EATKAIINYQ YNQYTEEEKN NINFNIDDLS SKLNESINKA 
781:	MININKFLNQ CSVSYLMNSM IPYGVKRLED FDASLKDALL KYIYDNRGTL IGQVDRLKDK 
841:	VNNTLSTDIP FQLSKYVDNQ RLLSTFTEYI KNIINTSILN LRYESNHLID LSRYASKINI 
901:	GSKVNFDPID KNQIQLFNLE SSKIEVILKN AIVYNSMYEN FSTSFWIRIP KYFNSISLNN 
961:	EYTIINCMEN NSGWKVSLNY GEIIWTLQDT QEIKQRVVFK YSQMINISDY INRWIFVTIT 
1021:	NNRLNNSKIY INGRLIDQKP ISNLGNIHAS NNIMFKLDGC RDTHRYIWIK YFNLFDKELN 
1081:	EKEIKDLYDN QSNSGILKDF WGDYLQYDKP YYMLNLYDPN KYVDVNNVGI RGYMYLKGPR 
1141:	GSVMTTNIYL NSSLYRGTKF IIKKYASGNK DNIVRNNDRV YINVVVKNKE YRLATNASQA 
1201:	GVEKILSALE IPDVGNLSQV VVMKSKNDQG ITNKCKMNLQ DNNGNDIGFI GFHQFNNIAK 
1261:	LVASNWYNRQ IERSSRTLGC SWEFIPVDDG WGERPL