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P04958 (TETX_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tetanus toxin
EC=3.4.24.68
Alternative name(s):
Tentoxylysin

Cleaved into the following 2 chains:

  1. Tetanus toxin light chain
    Short name=Tetanus toxin chain L
  2. Tetanus toxin heavy chain
    Short name=Tetanus toxin chain H
Gene names
Name:tetX
Ordered Locus Names:CTC_p60
Encoded onPlasmid pE88 Ref.3
Plasmid 75 Kbp Ref.1 Ref.2 Ref.4
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length1315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

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.

Miscellaneous

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

Sequence similarities

Belongs to the peptidase M27 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 457456Tetanus toxin light chain
PRO_0000029229
Chain458 – 1315858Tetanus toxin heavy chain
PRO_0000029230

Sites

Active site2341 By similarity
Metal binding2331Zinc; catalytic By similarity
Metal binding2371Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond439 ↔ 467Interchain (between light and heavy chains) Ref.5
Disulfide bond1077 ↔ 1093 Ref.5

Secondary structure

1 ........................................................................................................................................................................ 1315
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04958 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 18838FB2654024CF

FASTA1,315150,682
        10         20         30         40         50         60 
MPITINNFRY SDPVNNDTII MMEPPYCKGL DIYYKAFKIT DRIWIVPERY EFGTKPEDFN 

        70         80         90        100        110        120 
PPSSLIEGAS EYYDPNYLRT DSDKDRFLQT MVKLFNRIKN NVAGEALLDK IINAIPYLGN 

       130        140        150        160        170        180 
SYSLLDKFDT NSNSVSFNLL EQDPSGATTK SAMLTNLIIF GPGPVLNKNE VRGIVLRVDN 

       190        200        210        220        230        240 
KNYFPCRDGF GSIMQMAFCP EYVPTFDNVI ENITSLTIGK SKYFQDPALL LMHELIHVLH 

       250        260        270        280        290        300 
GLYGMQVSSH EIIPSKQEIY MQHTYPISAE ELFTFGGQDA NLISIDIKND LYEKTLNDYK 

       310        320        330        340        350        360 
AIANKLSQVT SCNDPNIDID SYKQIYQQKY QFDKDSNGQY IVNEDKFQIL YNSIMYGFTE 

       370        380        390        400        410        420 
IELGKKFNIK TRLSYFSMNH DPVKIPNLLD DTIYNDTEGF NIESKDLKSE YKGQNMRVNT 

       430        440        450        460        470        480 
NAFRNVDGSG LVSKLIGLCK KIIPPTNIRE NLYNRTASLT DLGGELCIKI KNEDLTFIAE 

       490        500        510        520        530        540 
KNSFSEEPFQ DEIVSYNTKN KPLNFNYSLD KIIVDYNLQS KITLPNDRTT PVTKGIPYAP 

       550        560        570        580        590        600 
EYKSNAASTI EIHNIDDNTI YQYLYAQKSP TTLQRITMTN SVDDALINST KIYSYFPSVI 

       610        620        630        640        650        660 
SKVNQGAQGI LFLQWVRDII DDFTNESSQK TTIDKISDVS TIVPYIGPAL NIVKQGYEGN 

       670        680        690        700        710        720 
FIGALETTGV VLLLEYIPEI TLPVIAALSI AESSTQKEKI IKTIDNFLEK RYEKWIEVYK 

       730        740        750        760        770        780 
LVKAKWLGTV NTQFQKRSYQ MYRSLEYQVD AIKKIIDYEY KIYSGPDKEQ IADEINNLKN 

       790        800        810        820        830        840 
KLEEKANKAM ININIFMRES SRSFLVNQMI NEAKKQLLEF DTQSKNILMQ YIKANSKFIG 

       850        860        870        880        890        900 
ITELKKLESK INKVFSTPIP FSYSKNLDCW VDNEEDIDVI LKKSTILNLD INNDIISDIS 

       910        920        930        940        950        960 
GFNSSVITYP DAQLVPGING KAIHLVNNES SEVIVHKAMD IEYNDMFNNF TVSFWLRVPK 

       970        980        990       1000       1010       1020 
VSASHLEQYG TNEYSIISSM KKHSLSIGSG WSVSLKGNNL IWTLKDSAGE VRQITFRDLP 

      1030       1040       1050       1060       1070       1080 
DKFNAYLANK WVFITITNDR LSSANLYING VLMGSAEITG LGAIREDNNI TLKLDRCNNN 

      1090       1100       1110       1120       1130       1140 
NQYVSIDKFR IFCKALNPKE IEKLYTSYLS ITFLRDFWGN PLRYDTEYYL IPVASSSKDV 

      1150       1160       1170       1180       1190       1200 
QLKNITDYMY LTNAPSYTNG KLNIYYRRLY NGLKFIIKRY TPNNEIDSFV KSGDFIKLYV 

      1210       1220       1230       1240       1250       1260 
SYNNNEHIVG YPKDGNAFNN LDRILRVGYN APGIPLYKKM EAVKLRDLKT YSVQLKLYDD 

      1270       1280       1290       1300       1310 
KNASLGLVGT HNGQIGNDPN RDILIASNWY FNHLKDKILG CDWYFVPTDE GWTND

« Hide

References

« Hide 'large scale' references
[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].
[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.
[3]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.
[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.
[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.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

Tetanus toxin Hc fragment

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X04436 Genomic DNA. Translation: CAA28033.1.
X06214 Genomic DNA. Translation: CAA29564.1.
AF528097 Genomic DNA. Translation: AAO37454.1.
M12739 Genomic DNA. Translation: AAA23282.1.
PIRBTCLTN. A25689.
RefSeqNP_783831.1. NC_004565.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8DX-ray1.57A865-1314[»]
1AF9X-ray2.70A865-1315[»]
1D0HX-ray2.10A872-1315[»]
1DFQX-ray2.60A872-1314[»]
1DIWX-ray2.00A875-1314[»]
1DLLX-ray1.80A875-1314[»]
1FV2X-ray2.50A865-1314[»]
1FV3X-ray2.30A/B865-1314[»]
1YVGX-ray2.60A2-458[»]
1YXWX-ray2.20A875-1314[»]
1YYNX-ray2.30A875-1314[»]
1Z7HX-ray2.30A1-443[»]
3HMYX-ray2.00A866-1315[»]
3HN1X-ray2.10A866-1315[»]
ProteinModelPortalP04958.
SMRP04958. Positions 2-427, 865-1315.
ModBaseSearch...

Protein-protein interaction databases

STRING212717.pE88_60.

Protein family/group databases

Allergome2757. Clo t Toxoid.
MEROPSM27.001.
TCDB1.C.8.1.2. botulinum and tetanus toxin (BTT) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO37454; AAO37454; CTC_p60.
GeneID1061100.
KEGGctc:pE88_60.
PATRIC19513592. VBICloTet101274_2814.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG12793.
KOK08644.
OMAMHELIHV.
ProtClustDBCLSK912378.

Enzyme and pathway databases

BioCycCTET212717:GJAM-2513-MONOMER.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProIPR008985. 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]
PfamPF01742. 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]
PRINTSPR00760. BONTOXILYSIN.
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
SSF50386. Kunitz_like. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP04958.
ChEMBLCHEMBL2036.
EvolutionaryTraceP04958.
PMAP-CutDBP04958.

Entry information

Entry nameTETX_CLOTE
AccessionPrimary (citable) accession number: P04958
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents