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P19321

- BXD_CLOBO

UniProt

P19321 - BXD_CLOBO

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Protein

Botulinum neurotoxin type D

Gene
botD
Organism
Clostridium botulinum
Status
Reviewed - Annotation score: 5 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 that cleaves the '60-Lys-|-Leu-61' bond of synaptobrevins-1 and -2.

Catalytic activityi

Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi229 – 2291Zinc; catalytic
Active sitei230 – 2301 By similarity
Metal bindingi233 – 2331Zinc; catalytic
Metal bindingi269 – 2691Zinc; catalytic

GO - Molecular functioni

  1. metalloendopeptidase activity Source: Reactome
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. inhibition of neurotransmitter uptake Source: InterPro
  2. neurotransmitter secretion Source: Reactome
  3. pathogenesis Source: UniProtKB-KW
  4. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_200617. Toxicity of botulinum toxin type D (BoNT/D).

Protein family/group databases

MEROPSiM27.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Botulinum neurotoxin type D (EC:3.4.24.69)
Short name:
BoNT/D
Alternative name(s):
Bontoxilysin-D
Cleaved into the following 2 chains:
Gene namesi
Name:botD
OrganismiClostridium botulinum
Taxonomic identifieri1491 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

  1. host cell cytosol Source: UniProtKB-SubCell
  2. host cell junction Source: UniProtKB-KW
  3. host cell presynaptic membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell junction, Host cell membrane, Host cytoplasm, Host membrane, Host synapse, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 442442Botulinum neurotoxin D light chainPRO_0000029219Add
BLAST
Chaini443 – 1276834Botulinum neurotoxin D heavy chainPRO_0000029220Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi437 ↔ 450Interchain (between light and heavy chains) Inferred

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.

Structurei

Secondary structure

1
1276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 238
Beta strandi34 – 407
Beta strandi43 – 464
Turni67 – 693
Turni74 – 774
Helixi80 – 9718
Helixi101 – 11212
Beta strandi126 – 1283
Turni132 – 1343
Beta strandi136 – 1427
Beta strandi145 – 1528
Beta strandi155 – 1595
Helixi181 – 1833
Beta strandi184 – 1863
Beta strandi190 – 1934
Beta strandi201 – 2033
Beta strandi218 – 2203
Helixi223 – 23816
Helixi267 – 2737
Helixi275 – 2806
Helixi283 – 30624
Beta strandi309 – 3124
Helixi313 – 3186
Helixi319 – 32911
Helixi344 – 35512
Helixi360 – 3667
Turni390 – 3923
Turni395 – 3973
Helixi403 – 4053
Helixi411 – 4133
Turni415 – 4173
Beta strandi421 – 4233
Helixi864 – 8674
Beta strandi868 – 8758
Beta strandi878 – 8814
Beta strandi883 – 8853
Beta strandi888 – 8914
Beta strandi896 – 9016
Beta strandi904 – 9074
Beta strandi909 – 9113
Beta strandi914 – 9174
Beta strandi931 – 9399
Helixi941 – 9444
Beta strandi948 – 9547
Beta strandi957 – 9593
Beta strandi961 – 9677
Beta strandi970 – 9767
Beta strandi982 – 9887
Turni991 – 9933
Beta strandi1003 – 10097
Beta strandi1013 – 10197
Beta strandi1022 – 10287
Beta strandi1040 – 10445
Beta strandi1055 – 106511
Helixi1069 – 107911
Turni1080 – 10834
Beta strandi1090 – 10923
Beta strandi1098 – 11036
Beta strandi1109 – 11146
Beta strandi1117 – 11226
Beta strandi1135 – 11395
Beta strandi1150 – 11523
Beta strandi1154 – 11618
Beta strandi1164 – 11707
Beta strandi1188 – 11969
Helixi1201 – 12033
Beta strandi1204 – 12096
Beta strandi1218 – 12225
Beta strandi1224 – 12263
Beta strandi1228 – 12358
Beta strandi1245 – 12539
Helixi1255 – 12573
Helixi1261 – 12633
Beta strandi1265 – 12684

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FPQX-ray1.65A1-436[»]
3N7JX-ray2.00A862-1276[»]
3OBRX-ray1.72A863-1276[»]
3OBTX-ray2.00A863-1276[»]
3OGGX-ray1.65A863-1276[»]
3RMXX-ray2.75A/B/C/D862-1276[»]
3RMYX-ray2.30A/B/C/D862-1276[»]
ProteinModelPortaliP19321.

Miscellaneous databases

EvolutionaryTraceiP19321.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.

Keywords - Domaini

Transmembrane

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR011065. Kunitz_inhibitor_ST1-like.
IPR000395. Neurotox_Zn_protease.
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. 2 hits.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19321-1 [UniParc]FASTAAdd to Basket

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MTWPVKDFNY SDPVNDNDIL YLRIPQNKLI TTPVKAFMIT QNIWVIPERF     50
SSDTNPSLSK PPRPTSKYQS YYDPSYLSTD EQKDTFLKGI IKLFKRINER 100
DIGKKLINYL VVGSPFMGDS STPEDTFDFT RHTTNIAVEK FENGSWKVTN 150
IITPSVLIFG PLPNILDYTA SLTLQGQQSN PSFEGFGTLS ILKVAPEFLL 200
TFSDVTSNQS SAVLGKSIFC MDPVIALMHE LTHSLHQLYG INIPSDKRIR 250
PQVSEGFFSQ DGPNVQFEEL YTFGGLDVEI IPQIERSQLR EKALGHYKDI 300
AKRLNNINKT IPSSWISNID KYKKIFSEKY NFDKDNTGNF VVNIDKFNSL 350
YSDLTNVMSE VVYSSQYNVK NRTHYFSRHY LPVFANILDD NIYTIRDGFN 400
LTNKGFNIEN SGQNIERNPA LQKLSSESVV DLFTKVCLRL TKNSRDDSTC 450
IKVKNNRLPY VADKDSISQE IFENKIITDE TNVQNYSDKF SLDESILDGQ 500
VPINPEIVDP LLPNVNMEPL NLPGEEIVFY DDITKYVDYL NSYYYLESQK 550
LSNNVENITL TTSVEEALGY SNKIYTFLPS LAEKVNKGVQ AGLFLNWANE 600
VVEDFTTNIM KKDTLDKISD VSVIIPYIGP ALNIGNSALR GNFNQAFATA 650
GVAFLLEGFP EFTIPALGVF TFYSSIQERE KIIKTIENCL EQRVKRWKDS 700
YQWMVSNWLS RITTQFNHIN YQMYDSLSYQ ADAIKAKIDL EYKKYSGSDK 750
ENIKSQVENL KNSLDVKISE AMNNINKFIR ECSVTYLFKN MLPKVIDELN 800
KFDLRTKTEL INLIDSHNII LVGEVDRLKA KVNESFENTM PFNIFSYTNN 850
SLLKDIINEY FNSINDSKIL SLQNKKNALV DTSGYNAEVR VGDNVQLNTI 900
YTNDFKLSSS GDKIIVNLNN NILYSAIYEN SSVSFWIKIS KDLTNSHNEY 950
TIINSIEQNS GWKLCIRNGN IEWILQDVNR KYKSLIFDYS ESLSHTGYTN 1000
KWFFVTITNN IMGYMKLYIN GELKQSQKIE DLDEVKLDKT IVFGIDENID 1050
ENQMLWIRDF NIFSKELSNE DINIVYEGQI LRNVIKDYWG NPLKFDTEYY 1100
IINDNYIDRY IAPESNVLVL VQYPDRSKLY TGNPITIKSV SDKNPYSRIL 1150
NGDNIILHML YNSRKYMIIR DTDTIYATQG GECSQNCVYA LKLQSNLGNY 1200
GIGIFSIKNI VSKNKYCSQI FSSFRENTML LADIYKPWRF SFKNAYTPVA 1250
VTNYETKLLS TSSFWKFISR DPGWVE 1276
Length:1,276
Mass (Da):146,872
Last modified:November 1, 1990 - v1
Checksum:iC1EC50F46C8233E2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 162ND → PV in strain: D-SA.
Natural varianti17 – 182ND → LQ in strain: D-1873.
Natural varianti452 – 4521K → Q in strain: D-SA.
Natural varianti457 – 4571R → F in strain: D-1873.
Natural varianti457 – 4571R → T in strain: D-SA.
Natural varianti462 – 4621A → D in strain: D-1873.
Natural varianti489 – 4891K → N in strain: CB16.
Natural varianti644 – 6441N → K in strain: CB16.
Natural varianti1122 – 11221Q → R in strain: CB16.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54254 Genomic DNA. Translation: CAA38175.1.
S49407 Genomic DNA. Translation: AAB24244.1.
PIRiS11455.

Cross-referencesi

Web resourcesi

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54254 Genomic DNA. Translation: CAA38175.1 .
S49407 Genomic DNA. Translation: AAB24244.1 .
PIRi S11455.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FPQ X-ray 1.65 A 1-436 [» ]
3N7J X-ray 2.00 A 862-1276 [» ]
3OBR X-ray 1.72 A 863-1276 [» ]
3OBT X-ray 2.00 A 863-1276 [» ]
3OGG X-ray 1.65 A 863-1276 [» ]
3RMX X-ray 2.75 A/B/C/D 862-1276 [» ]
3RMY X-ray 2.30 A/B/C/D 862-1276 [» ]
ProteinModelPortali P19321.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M27.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

Reactomei REACT_200617. Toxicity of botulinum toxin type D (BoNT/D).

Miscellaneous databases

EvolutionaryTracei P19321.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR011065. Kunitz_inhibitor_ST1-like.
IPR000395. Neurotox_Zn_protease.
IPR013104. Toxin_rcpt-bd_C.
IPR012928. Toxin_rcpt-bd_N.
IPR012500. Toxin_trans.
[Graphical view ]
Pfami PF01742. 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 ]
PRINTSi PR00760. BONTOXILYSIN.
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF50386. SSF50386. 2 hits.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Type D / BVD/-3.
  2. "The complete amino acid sequence of the Clostridium botulinum type D neurotoxin, deduced by nucleotide sequence analysis of the encoding phage d-16 phi genome."
    Sunagawa H., Ohyama T., Watanabe T., Inoue K.
    J. Vet. Med. Sci. 54:905-913(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Type D / CB-16.
  3. "Molecular diversity of neurotoxins from Clostridium botulinum type D strains."
    Moriishi K., Syuto B., Kubo S., Oguma K.
    Infect. Immun. 57:2886-2891(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Strain: Type D / D-1873 and Type D / South African.
  4. "Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin."
    Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F., Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H.
    J. Biol. Chem. 269:12764-12772(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF SUBSTRATE.
  5. "Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity."
    Arndt J.W., Chai Q., Christian T., Stevens R.C.
    Biochemistry 45:3255-3262(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-436 IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiBXD_CLOBO
AccessioniPrimary (citable) accession number: P19321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: September 3, 2014
This is version 129 of the entry and version 1 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.
Botulinum type D neurotoxin is synthesized by D strains of C.botulinum which carry the appropriate bacteriophage.

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

External Data

Dasty 3

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