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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

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi229 – 2291Zinc; catalytic
Active sitei230 – 2301PROSITE-ProRule annotation
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 cytoplasm Source: UniProtKB-KW
  2. host cell junction Source: UniProtKB-KW
  3. host cell synapse Source: UniProtKB-KW
  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)Curated

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.1 Publication

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19321.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

Keywords - Domaini

Transmembrane

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
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

« Hide

        10         20         30         40         50
MTWPVKDFNY SDPVNDNDIL YLRIPQNKLI TTPVKAFMIT QNIWVIPERF
60 70 80 90 100
SSDTNPSLSK PPRPTSKYQS YYDPSYLSTD EQKDTFLKGI IKLFKRINER
110 120 130 140 150
DIGKKLINYL VVGSPFMGDS STPEDTFDFT RHTTNIAVEK FENGSWKVTN
160 170 180 190 200
IITPSVLIFG PLPNILDYTA SLTLQGQQSN PSFEGFGTLS ILKVAPEFLL
210 220 230 240 250
TFSDVTSNQS SAVLGKSIFC MDPVIALMHE LTHSLHQLYG INIPSDKRIR
260 270 280 290 300
PQVSEGFFSQ DGPNVQFEEL YTFGGLDVEI IPQIERSQLR EKALGHYKDI
310 320 330 340 350
AKRLNNINKT IPSSWISNID KYKKIFSEKY NFDKDNTGNF VVNIDKFNSL
360 370 380 390 400
YSDLTNVMSE VVYSSQYNVK NRTHYFSRHY LPVFANILDD NIYTIRDGFN
410 420 430 440 450
LTNKGFNIEN SGQNIERNPA LQKLSSESVV DLFTKVCLRL TKNSRDDSTC
460 470 480 490 500
IKVKNNRLPY VADKDSISQE IFENKIITDE TNVQNYSDKF SLDESILDGQ
510 520 530 540 550
VPINPEIVDP LLPNVNMEPL NLPGEEIVFY DDITKYVDYL NSYYYLESQK
560 570 580 590 600
LSNNVENITL TTSVEEALGY SNKIYTFLPS LAEKVNKGVQ AGLFLNWANE
610 620 630 640 650
VVEDFTTNIM KKDTLDKISD VSVIIPYIGP ALNIGNSALR GNFNQAFATA
660 670 680 690 700
GVAFLLEGFP EFTIPALGVF TFYSSIQERE KIIKTIENCL EQRVKRWKDS
710 720 730 740 750
YQWMVSNWLS RITTQFNHIN YQMYDSLSYQ ADAIKAKIDL EYKKYSGSDK
760 770 780 790 800
ENIKSQVENL KNSLDVKISE AMNNINKFIR ECSVTYLFKN MLPKVIDELN
810 820 830 840 850
KFDLRTKTEL INLIDSHNII LVGEVDRLKA KVNESFENTM PFNIFSYTNN
860 870 880 890 900
SLLKDIINEY FNSINDSKIL SLQNKKNALV DTSGYNAEVR VGDNVQLNTI
910 920 930 940 950
YTNDFKLSSS GDKIIVNLNN NILYSAIYEN SSVSFWIKIS KDLTNSHNEY
960 970 980 990 1000
TIINSIEQNS GWKLCIRNGN IEWILQDVNR KYKSLIFDYS ESLSHTGYTN
1010 1020 1030 1040 1050
KWFFVTITNN IMGYMKLYIN GELKQSQKIE DLDEVKLDKT IVFGIDENID
1060 1070 1080 1090 1100
ENQMLWIRDF NIFSKELSNE DINIVYEGQI LRNVIKDYWG NPLKFDTEYY
1110 1120 1130 1140 1150
IINDNYIDRY IAPESNVLVL VQYPDRSKLY TGNPITIKSV SDKNPYSRIL
1160 1170 1180 1190 1200
NGDNIILHML YNSRKYMIIR DTDTIYATQG GECSQNCVYA LKLQSNLGNY
1210 1220 1230 1240 1250
GIGIFSIKNI VSKNKYCSQI FSSFRENTML LADIYKPWRF SFKNAYTPVA
1260 1270
VTNYETKLLS TSSFWKFISR DPGWVE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X54254 Genomic DNA. Translation: CAA38175.1 .
S49407 Genomic DNA. Translation: AAB24244.1 .
PIRi S11455.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 IPR013320. ConA-like_dom.
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: November 26, 2014
This is version 132 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