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P04958

- TETX_CLOTE

UniProt

P04958 - TETX_CLOTE

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Protein
Tetanus toxin
Gene
tetX, CTC_p60
Organism
Clostridium tetani (strain Massachusetts / E88)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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; catalytic By similarity
Active sitei234 – 2341 By similarity
Metal bindingi237 – 2371Zinc; catalytic By similarity

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
Complete GO annotation...

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
Complete GO annotation...

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 chain
PRO_0000029229Add
BLAST
Chaini458 – 1315858Tetanus toxin heavy chain
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP04958.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 132 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

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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