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P04958

- TETX_CLOTE

UniProt

P04958 - TETX_CLOTE

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Protein

Tetanus toxin

Gene

tetX

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

Zn2+By similarityNote: 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
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 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 – 238Combined sources
Helixi25 – 273Combined sources
Turni28 – 303Combined sources
Beta strandi34 – 407Combined sources
Beta strandi43 – 464Combined sources
Helixi56 – 594Combined sources
Turni75 – 784Combined sources
Helixi81 – 9919Combined sources
Helixi102 – 11312Combined sources
Turni133 – 1353Combined sources
Beta strandi136 – 1438Combined sources
Turni144 – 1463Combined sources
Beta strandi147 – 1548Combined sources
Beta strandi156 – 1605Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi181 – 1833Combined sources
Helixi185 – 1873Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi194 – 1974Combined sources
Beta strandi200 – 2034Combined sources
Helixi227 – 24216Combined sources
Helixi269 – 2757Combined sources
Helixi277 – 2826Combined sources
Helixi285 – 30622Combined sources
Beta strandi311 – 3133Combined sources
Helixi319 – 33012Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi340 – 3423Combined sources
Helixi344 – 35512Combined sources
Helixi360 – 3678Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi380 – 3845Combined sources
Turni386 – 3894Combined sources
Turni391 – 3933Combined sources
Turni396 – 3983Combined sources
Helixi403 – 4053Combined sources
Helixi409 – 4146Combined sources
Turni416 – 4183Combined sources
Helixi420 – 4223Combined sources
Helixi877 – 8837Combined sources
Beta strandi885 – 8928Combined sources
Beta strandi895 – 8984Combined sources
Beta strandi900 – 9023Combined sources
Beta strandi905 – 9084Combined sources
Beta strandi913 – 9164Combined sources
Beta strandi918 – 92811Combined sources
Beta strandi933 – 9364Combined sources
Helixi939 – 9413Combined sources
Turni942 – 9476Combined sources
Beta strandi950 – 9578Combined sources
Helixi963 – 9697Combined sources
Beta strandi973 – 9786Combined sources
Helixi984 – 9863Combined sources
Beta strandi988 – 9969Combined sources
Beta strandi999 – 10057Combined sources
Turni1007 – 10093Combined sources
Beta strandi1011 – 10177Combined sources
Turni1022 – 10243Combined sources
Beta strandi1026 – 10305Combined sources
Beta strandi1032 – 10387Combined sources
Beta strandi1042 – 10487Combined sources
Beta strandi1051 – 10577Combined sources
Beta strandi1068 – 10769Combined sources
Beta strandi1083 – 109412Combined sources
Helixi1098 – 11069Combined sources
Beta strandi1111 – 11133Combined sources
Beta strandi1119 – 11213Combined sources
Beta strandi1123 – 11253Combined sources
Beta strandi1128 – 11325Combined sources
Helixi1133 – 11353Combined sources
Beta strandi1138 – 11447Combined sources
Beta strandi1149 – 11535Combined sources
Beta strandi1156 – 11594Combined sources
Turni1160 – 11634Combined sources
Beta strandi1164 – 11674Combined sources
Beta strandi1174 – 11818Combined sources
Beta strandi1194 – 12029Combined sources
Beta strandi1205 – 12128Combined sources
Turni1219 – 12213Combined sources
Beta strandi1222 – 12243Combined sources
Beta strandi1226 – 12283Combined sources
Beta strandi1239 – 12435Combined sources
Beta strandi1253 – 12586Combined sources
Beta strandi1260 – 12623Combined sources
Beta strandi1264 – 127310Combined sources
Beta strandi1281 – 12877Combined sources
Helixi1288 – 12936Combined sources
Beta strandi1296 – 12983Combined sources
Beta strandi1303 – 13064Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
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. 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

        10         20         30         40         50
MPITINNFRY SDPVNNDTII MMEPPYCKGL DIYYKAFKIT DRIWIVPERY
60 70 80 90 100
EFGTKPEDFN PPSSLIEGAS EYYDPNYLRT DSDKDRFLQT MVKLFNRIKN
110 120 130 140 150
NVAGEALLDK IINAIPYLGN SYSLLDKFDT NSNSVSFNLL EQDPSGATTK
160 170 180 190 200
SAMLTNLIIF GPGPVLNKNE VRGIVLRVDN KNYFPCRDGF GSIMQMAFCP
210 220 230 240 250
EYVPTFDNVI ENITSLTIGK SKYFQDPALL LMHELIHVLH GLYGMQVSSH
260 270 280 290 300
EIIPSKQEIY MQHTYPISAE ELFTFGGQDA NLISIDIKND LYEKTLNDYK
310 320 330 340 350
AIANKLSQVT SCNDPNIDID SYKQIYQQKY QFDKDSNGQY IVNEDKFQIL
360 370 380 390 400
YNSIMYGFTE IELGKKFNIK TRLSYFSMNH DPVKIPNLLD DTIYNDTEGF
410 420 430 440 450
NIESKDLKSE YKGQNMRVNT NAFRNVDGSG LVSKLIGLCK KIIPPTNIRE
460 470 480 490 500
NLYNRTASLT DLGGELCIKI KNEDLTFIAE KNSFSEEPFQ DEIVSYNTKN
510 520 530 540 550
KPLNFNYSLD KIIVDYNLQS KITLPNDRTT PVTKGIPYAP EYKSNAASTI
560 570 580 590 600
EIHNIDDNTI YQYLYAQKSP TTLQRITMTN SVDDALINST KIYSYFPSVI
610 620 630 640 650
SKVNQGAQGI LFLQWVRDII DDFTNESSQK TTIDKISDVS TIVPYIGPAL
660 670 680 690 700
NIVKQGYEGN FIGALETTGV VLLLEYIPEI TLPVIAALSI AESSTQKEKI
710 720 730 740 750
IKTIDNFLEK RYEKWIEVYK LVKAKWLGTV NTQFQKRSYQ MYRSLEYQVD
760 770 780 790 800
AIKKIIDYEY KIYSGPDKEQ IADEINNLKN KLEEKANKAM ININIFMRES
810 820 830 840 850
SRSFLVNQMI NEAKKQLLEF DTQSKNILMQ YIKANSKFIG ITELKKLESK
860 870 880 890 900
INKVFSTPIP FSYSKNLDCW VDNEEDIDVI LKKSTILNLD INNDIISDIS
910 920 930 940 950
GFNSSVITYP DAQLVPGING KAIHLVNNES SEVIVHKAMD IEYNDMFNNF
960 970 980 990 1000
TVSFWLRVPK VSASHLEQYG TNEYSIISSM KKHSLSIGSG WSVSLKGNNL
1010 1020 1030 1040 1050
IWTLKDSAGE VRQITFRDLP DKFNAYLANK WVFITITNDR LSSANLYING
1060 1070 1080 1090 1100
VLMGSAEITG LGAIREDNNI TLKLDRCNNN NQYVSIDKFR IFCKALNPKE
1110 1120 1130 1140 1150
IEKLYTSYLS ITFLRDFWGN PLRYDTEYYL IPVASSSKDV QLKNITDYMY
1160 1170 1180 1190 1200
LTNAPSYTNG KLNIYYRRLY NGLKFIIKRY TPNNEIDSFV KSGDFIKLYV
1210 1220 1230 1240 1250
SYNNNEHIVG YPKDGNAFNN LDRILRVGYN APGIPLYKKM EAVKLRDLKT
1260 1270 1280 1290 1300
YSVQLKLYDD KNASLGLVGT HNGQIGNDPN RDILIASNWY FNHLKDKILG
1310
CDWYFVPTDE GWTND
Length:1,315
Mass (Da):150,682
Last modified:January 23, 2007 - v2
Checksum:i18838FB2654024CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 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. 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: November 26, 2014
This is version 135 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