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P04958

- TETX_CLOTE

UniProt

P04958 - TETX_CLOTE

Protein

Tetanus toxin

Gene

tetX

Organism
Clostridium tetani (strain Massachusetts / E88)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Tetanus 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 catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of synaptobrevin-2.

    Catalytic activityi

    Hydrolysis of 76-Gln-|-Phe-77 bond in synaptobrevin 2.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi233 – 2331Zinc; catalyticPROSITE-ProRule annotation
    Active sitei234 – 2341PROSITE-ProRule annotation
    Metal bindingi237 – 2371Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. inhibition of neurotransmitter uptake Source: InterPro
    2. negative regulation of neurotransmitter secretion Source: CACAO
    3. pathogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciCTET212717:GJAM-2513-MONOMER.

    Protein family/group databases

    MEROPSiM27.001.
    TCDBi1.C.8.1.2. the botulinum and tetanus toxin (btt) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tetanus toxin (EC:3.4.24.68)
    Alternative name(s):
    Tentoxylysin
    Cleaved into the following 2 chains:
    Tetanus toxin light chain
    Short name:
    Tetanus toxin chain L
    Tetanus toxin heavy chain
    Short name:
    Tetanus toxin chain H
    Gene namesi
    Name:tetX
    Ordered Locus Names:CTC_p60
    Encoded oniPlasmid pE881 Publication
    Plasmid 75 Kbp3 Publications
    OrganismiClostridium tetani (strain Massachusetts / E88)
    Taxonomic identifieri212717 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000001412: Plasmid pE88

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    Pathology & Biotechi

    Protein family/group databases

    Allergomei2757. Clo t Toxoid.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 457456Tetanus toxin light chainPRO_0000029229Add
    BLAST
    Chaini458 – 1315858Tetanus toxin heavy chainPRO_0000029230Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi439 ↔ 467Interchain (between light and heavy chains)1 Publication
    Disulfide bondi1077 ↔ 10931 Publication

    Keywords - PTMi

    Disulfide bond

    Miscellaneous databases

    PMAP-CutDBP04958.

    Interactioni

    Subunit structurei

    The precursor polypeptide is subsequently cleaved to yield subchains L and H. These remain linked by a disulfide bridge and are non-toxic after separation.

    Protein-protein interaction databases

    STRINGi212717.pE88_60.

    Structurei

    Secondary structure

    1
    1315
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 238
    Helixi25 – 273
    Turni28 – 303
    Beta strandi34 – 407
    Beta strandi43 – 464
    Helixi56 – 594
    Turni75 – 784
    Helixi81 – 9919
    Helixi102 – 11312
    Turni133 – 1353
    Beta strandi136 – 1438
    Turni144 – 1463
    Beta strandi147 – 1548
    Beta strandi156 – 1605
    Beta strandi170 – 1734
    Beta strandi176 – 1783
    Beta strandi181 – 1833
    Helixi185 – 1873
    Beta strandi188 – 1903
    Beta strandi194 – 1974
    Beta strandi200 – 2034
    Helixi227 – 24216
    Helixi269 – 2757
    Helixi277 – 2826
    Helixi285 – 30622
    Beta strandi311 – 3133
    Helixi319 – 33012
    Beta strandi332 – 3343
    Beta strandi336 – 3383
    Beta strandi340 – 3423
    Helixi344 – 35512
    Helixi360 – 3678
    Beta strandi373 – 3753
    Beta strandi380 – 3845
    Turni386 – 3894
    Turni391 – 3933
    Turni396 – 3983
    Helixi403 – 4053
    Helixi409 – 4146
    Turni416 – 4183
    Helixi420 – 4223
    Helixi877 – 8837
    Beta strandi885 – 8928
    Beta strandi895 – 8984
    Beta strandi900 – 9023
    Beta strandi905 – 9084
    Beta strandi913 – 9164
    Beta strandi918 – 92811
    Beta strandi933 – 9364
    Helixi939 – 9413
    Turni942 – 9476
    Beta strandi950 – 9578
    Helixi963 – 9697
    Beta strandi973 – 9786
    Helixi984 – 9863
    Beta strandi988 – 9969
    Beta strandi999 – 10057
    Turni1007 – 10093
    Beta strandi1011 – 10177
    Turni1022 – 10243
    Beta strandi1026 – 10305
    Beta strandi1032 – 10387
    Beta strandi1042 – 10487
    Beta strandi1051 – 10577
    Beta strandi1068 – 10769
    Beta strandi1083 – 109412
    Helixi1098 – 11069
    Beta strandi1111 – 11133
    Beta strandi1119 – 11213
    Beta strandi1123 – 11253
    Beta strandi1128 – 11325
    Helixi1133 – 11353
    Beta strandi1138 – 11447
    Beta strandi1149 – 11535
    Beta strandi1156 – 11594
    Turni1160 – 11634
    Beta strandi1164 – 11674
    Beta strandi1174 – 11818
    Beta strandi1194 – 12029
    Beta strandi1205 – 12128
    Turni1219 – 12213
    Beta strandi1222 – 12243
    Beta strandi1226 – 12283
    Beta strandi1239 – 12435
    Beta strandi1253 – 12586
    Beta strandi1260 – 12623
    Beta strandi1264 – 127310
    Beta strandi1281 – 12877
    Helixi1288 – 12936
    Beta strandi1296 – 12983
    Beta strandi1303 – 13064

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A8DX-ray1.57A865-1315[»]
    1AF9X-ray2.70A865-1315[»]
    1D0HX-ray2.10A872-1315[»]
    1DFQX-ray2.60A872-1315[»]
    1DIWX-ray2.00A875-1315[»]
    1DLLX-ray1.80A875-1315[»]
    1FV2X-ray2.50A862-1315[»]
    1FV3X-ray2.30A/B862-1315[»]
    1YVGX-ray2.60A2-458[»]
    1YXWX-ray2.20A875-1315[»]
    1YYNX-ray2.30A875-1315[»]
    1Z7HX-ray2.30A1-443[»]
    3HMYX-ray2.00A866-1315[»]
    3HN1X-ray2.10A866-1315[»]
    4J1LX-ray2.60A2-427[»]
    ProteinModelPortaliP04958.
    SMRiP04958. Positions 2-427, 865-1315.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04958.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M27 family.Curated

    Phylogenomic databases

    eggNOGiNOG12793.
    KOiK08644.
    OMAiKITDRIW.
    OrthoDBiEOG67T5DS.

    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. 1 hit.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P04958-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPITINNFRY SDPVNNDTII MMEPPYCKGL DIYYKAFKIT DRIWIVPERY     50
    EFGTKPEDFN PPSSLIEGAS EYYDPNYLRT DSDKDRFLQT MVKLFNRIKN 100
    NVAGEALLDK IINAIPYLGN SYSLLDKFDT NSNSVSFNLL EQDPSGATTK 150
    SAMLTNLIIF GPGPVLNKNE VRGIVLRVDN KNYFPCRDGF GSIMQMAFCP 200
    EYVPTFDNVI ENITSLTIGK SKYFQDPALL LMHELIHVLH GLYGMQVSSH 250
    EIIPSKQEIY MQHTYPISAE ELFTFGGQDA NLISIDIKND LYEKTLNDYK 300
    AIANKLSQVT SCNDPNIDID SYKQIYQQKY QFDKDSNGQY IVNEDKFQIL 350
    YNSIMYGFTE IELGKKFNIK TRLSYFSMNH DPVKIPNLLD DTIYNDTEGF 400
    NIESKDLKSE YKGQNMRVNT NAFRNVDGSG LVSKLIGLCK KIIPPTNIRE 450
    NLYNRTASLT DLGGELCIKI KNEDLTFIAE KNSFSEEPFQ DEIVSYNTKN 500
    KPLNFNYSLD KIIVDYNLQS KITLPNDRTT PVTKGIPYAP EYKSNAASTI 550
    EIHNIDDNTI YQYLYAQKSP TTLQRITMTN SVDDALINST KIYSYFPSVI 600
    SKVNQGAQGI LFLQWVRDII DDFTNESSQK TTIDKISDVS TIVPYIGPAL 650
    NIVKQGYEGN FIGALETTGV VLLLEYIPEI TLPVIAALSI AESSTQKEKI 700
    IKTIDNFLEK RYEKWIEVYK LVKAKWLGTV NTQFQKRSYQ MYRSLEYQVD 750
    AIKKIIDYEY KIYSGPDKEQ IADEINNLKN KLEEKANKAM ININIFMRES 800
    SRSFLVNQMI NEAKKQLLEF DTQSKNILMQ YIKANSKFIG ITELKKLESK 850
    INKVFSTPIP FSYSKNLDCW VDNEEDIDVI LKKSTILNLD INNDIISDIS 900
    GFNSSVITYP DAQLVPGING KAIHLVNNES SEVIVHKAMD IEYNDMFNNF 950
    TVSFWLRVPK VSASHLEQYG TNEYSIISSM KKHSLSIGSG WSVSLKGNNL 1000
    IWTLKDSAGE VRQITFRDLP DKFNAYLANK WVFITITNDR LSSANLYING 1050
    VLMGSAEITG LGAIREDNNI TLKLDRCNNN NQYVSIDKFR IFCKALNPKE 1100
    IEKLYTSYLS ITFLRDFWGN PLRYDTEYYL IPVASSSKDV QLKNITDYMY 1150
    LTNAPSYTNG KLNIYYRRLY NGLKFIIKRY TPNNEIDSFV KSGDFIKLYV 1200
    SYNNNEHIVG YPKDGNAFNN LDRILRVGYN APGIPLYKKM EAVKLRDLKT 1250
    YSVQLKLYDD KNASLGLVGT HNGQIGNDPN RDILIASNWY FNHLKDKILG 1300
    CDWYFVPTDE GWTND 1315
    Length:1,315
    Mass (Da):150,682
    Last modified:January 23, 2007 - v2
    Checksum:i18838FB2654024CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04436 Genomic DNA. Translation: CAA28033.1.
    X06214 Genomic DNA. Translation: CAA29564.1.
    AF528097 Genomic DNA. Translation: AAO37454.1.
    M12739 Genomic DNA. Translation: AAA23282.1.
    PIRiA25689. BTCLTN.
    RefSeqiNP_783831.1. NC_004565.1.
    WP_011100836.1. NC_004565.1.

    Genome annotation databases

    EnsemblBacteriaiAAO37454; AAO37454; CTC_p60.
    GeneIDi1061100.
    KEGGictc:pE88_60.
    PATRICi19513592. VBICloTet101274_2814.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Tetanus toxin Hc fragment

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04436 Genomic DNA. Translation: CAA28033.1 .
    X06214 Genomic DNA. Translation: CAA29564.1 .
    AF528097 Genomic DNA. Translation: AAO37454.1 .
    M12739 Genomic DNA. Translation: AAA23282.1 .
    PIRi A25689. BTCLTN.
    RefSeqi NP_783831.1. NC_004565.1.
    WP_011100836.1. NC_004565.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A8D X-ray 1.57 A 865-1315 [» ]
    1AF9 X-ray 2.70 A 865-1315 [» ]
    1D0H X-ray 2.10 A 872-1315 [» ]
    1DFQ X-ray 2.60 A 872-1315 [» ]
    1DIW X-ray 2.00 A 875-1315 [» ]
    1DLL X-ray 1.80 A 875-1315 [» ]
    1FV2 X-ray 2.50 A 862-1315 [» ]
    1FV3 X-ray 2.30 A/B 862-1315 [» ]
    1YVG X-ray 2.60 A 2-458 [» ]
    1YXW X-ray 2.20 A 875-1315 [» ]
    1YYN X-ray 2.30 A 875-1315 [» ]
    1Z7H X-ray 2.30 A 1-443 [» ]
    3HMY X-ray 2.00 A 866-1315 [» ]
    3HN1 X-ray 2.10 A 866-1315 [» ]
    4J1L X-ray 2.60 A 2-427 [» ]
    ProteinModelPortali P04958.
    SMRi P04958. Positions 2-427, 865-1315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 212717.pE88_60.

    Chemistry

    BindingDBi P04958.
    ChEMBLi CHEMBL2036.

    Protein family/group databases

    Allergomei 2757. Clo t Toxoid.
    MEROPSi M27.001.
    TCDBi 1.C.8.1.2. the botulinum and tetanus toxin (btt) family.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO37454 ; AAO37454 ; CTC_p60 .
    GeneIDi 1061100.
    KEGGi ctc:pE88_60.
    PATRICi 19513592. VBICloTet101274_2814.

    Phylogenomic databases

    eggNOGi NOG12793.
    KOi K08644.
    OMAi KITDRIW.
    OrthoDBi EOG67T5DS.

    Enzyme and pathway databases

    BioCyci CTET212717:GJAM-2513-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P04958.
    PMAP-CutDB P04958.

    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. 1 hit.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Tetanus toxin: primary structure, expression in E. coli, and homology with botulinum toxins."
      Eisel U., Jarausch W., Goretzki K., Henschen A., Engels J., Weller U., Hudel M., Habermann E., Niemann H.
      EMBO J. 5:2495-2502(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Plasmid: 75 Kbp
    2. "The complete nucleotide sequence of tetanus toxin."
      Fairweather N.F., Lyness V.A.
      Nucleic Acids Res. 14:7809-7812(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CN3911.
      Plasmid: 75 Kbp
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Massachusetts / E88.
      Plasmid: pE88
    4. "Cloning, nucleotide sequencing, and expression of tetanus toxin fragment C in Escherichia coli."
      Fairweather N.F., Lyness V.A., Pickard D.J., Allen G., Thomson R.O.
      J. Bacteriol. 165:21-27(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 743-1315.
      Plasmid: 75 Kbp
    5. "Arrangement of disulfide bridges and positions of sulfhydryl groups in tetanus toxin."
      Krieglstein K., Henschen A., Weller U., Habermann E.
      Eur. J. Biochem. 188:39-45(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
    6. "Limited proteolysis of tetanus toxin. Relation to activity and identification of cleavage sites."
      Krieglstein K.G., Henschen A.H., Weller U., Habermann E.
      Eur. J. Biochem. 202:41-51(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    7. "Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc."
      Schiavo G., Poulain B., Rossetto O., Benfenati F., Tauc L., Montecucco C.
      EMBO J. 11:3577-3583(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A ZINC-PROTEASE.
    8. "Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin."
      Schiavo G., Benfenati F., Poulain B., Rossetto O., de Laureto P.P., Dasgupta B.R., Montecucco C.
      Nature 359:832-835(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF SUBSTRATE.
    9. "Structure of the receptor binding fragment HC of tetanus neurotoxin."
      Umland T.C., Wingert L.M., Swaminathan S., Furey W.F. Jr., Schmidt J.J., Sax M.
      Nat. Struct. Biol. 4:788-792(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 875-1315.

    Entry informationi

    Entry nameiTETX_CLOTE
    AccessioniPrimary (citable) accession number: P04958
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The C-terminus of the heavy chain binds to ganglioside receptors.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

    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