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Protein

Tetanus toxin

Gene

tetX

Organism
Clostridium tetani (strain Massachusetts / E88)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi233Zinc; catalyticPROSITE-ProRule annotation1
Active sitei234PROSITE-ProRule annotation1
Metal bindingi237Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.68. 1526.
ReactomeiR-HSA-5250982. Toxicity of tetanus toxin (TeNT).

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
Proteomesi
  • UP000001412 Componenti: Plasmid pE88

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Protein family/group databases

Allergomei2757. Clo t Toxoid.

Chemistry databases

ChEMBLiCHEMBL2036.
DrugBankiDB04465. Lactose.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000292292 – 457Tetanus toxin light chainAdd BLAST456
ChainiPRO_0000029230458 – 1315Tetanus toxin heavy chainAdd BLAST858

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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.

Chemistry databases

BindingDBiP04958.

Structurei

Secondary structure

11315
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 23Combined sources8
Helixi25 – 27Combined sources3
Turni28 – 30Combined sources3
Beta strandi34 – 40Combined sources7
Beta strandi43 – 46Combined sources4
Helixi56 – 59Combined sources4
Turni75 – 78Combined sources4
Helixi81 – 99Combined sources19
Helixi102 – 113Combined sources12
Turni133 – 135Combined sources3
Beta strandi136 – 143Combined sources8
Turni144 – 146Combined sources3
Beta strandi147 – 154Combined sources8
Beta strandi156 – 160Combined sources5
Beta strandi170 – 173Combined sources4
Beta strandi176 – 178Combined sources3
Beta strandi181 – 183Combined sources3
Helixi185 – 187Combined sources3
Beta strandi188 – 190Combined sources3
Beta strandi194 – 197Combined sources4
Beta strandi200 – 203Combined sources4
Helixi227 – 242Combined sources16
Helixi269 – 275Combined sources7
Helixi277 – 282Combined sources6
Helixi285 – 306Combined sources22
Beta strandi311 – 313Combined sources3
Helixi319 – 330Combined sources12
Beta strandi332 – 334Combined sources3
Beta strandi336 – 338Combined sources3
Beta strandi340 – 342Combined sources3
Helixi344 – 355Combined sources12
Helixi360 – 367Combined sources8
Beta strandi373 – 375Combined sources3
Beta strandi380 – 384Combined sources5
Turni386 – 389Combined sources4
Turni391 – 393Combined sources3
Turni396 – 398Combined sources3
Helixi403 – 405Combined sources3
Helixi409 – 414Combined sources6
Turni416 – 418Combined sources3
Helixi420 – 422Combined sources3
Helixi877 – 883Combined sources7
Beta strandi885 – 892Combined sources8
Beta strandi895 – 898Combined sources4
Beta strandi900 – 902Combined sources3
Beta strandi905 – 908Combined sources4
Beta strandi913 – 916Combined sources4
Beta strandi918 – 928Combined sources11
Beta strandi933 – 936Combined sources4
Helixi939 – 941Combined sources3
Turni942 – 947Combined sources6
Beta strandi950 – 957Combined sources8
Helixi963 – 969Combined sources7
Beta strandi973 – 978Combined sources6
Helixi984 – 986Combined sources3
Beta strandi988 – 996Combined sources9
Beta strandi999 – 1005Combined sources7
Turni1007 – 1009Combined sources3
Beta strandi1011 – 1017Combined sources7
Turni1022 – 1024Combined sources3
Beta strandi1026 – 1030Combined sources5
Beta strandi1032 – 1038Combined sources7
Beta strandi1042 – 1048Combined sources7
Beta strandi1051 – 1057Combined sources7
Beta strandi1068 – 1076Combined sources9
Beta strandi1083 – 1094Combined sources12
Helixi1098 – 1106Combined sources9
Beta strandi1111 – 1113Combined sources3
Beta strandi1119 – 1121Combined sources3
Beta strandi1123 – 1125Combined sources3
Beta strandi1128 – 1132Combined sources5
Helixi1133 – 1135Combined sources3
Beta strandi1138 – 1144Combined sources7
Beta strandi1149 – 1153Combined sources5
Beta strandi1156 – 1159Combined sources4
Turni1160 – 1163Combined sources4
Beta strandi1164 – 1167Combined sources4
Beta strandi1174 – 1181Combined sources8
Beta strandi1194 – 1202Combined sources9
Beta strandi1205 – 1212Combined sources8
Turni1219 – 1221Combined sources3
Beta strandi1222 – 1224Combined sources3
Beta strandi1226 – 1228Combined sources3
Beta strandi1239 – 1243Combined sources5
Beta strandi1253 – 1258Combined sources6
Beta strandi1260 – 1262Combined sources3
Beta strandi1264 – 1273Combined sources10
Beta strandi1281 – 1287Combined sources7
Helixi1288 – 1293Combined sources6
Beta strandi1296 – 1298Combined sources3
Beta strandi1303 – 1306Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP04958.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

Phylogenomic databases

KOiK08644.
OMAiDFWGNPL.
OrthoDBiPOG091H19UB.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
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.
RefSeqiWP_011100836.1. NC_004565.1.

Genome annotation databases

EnsemblBacteriaiAAO37454; AAO37454; CTC_p60.
GeneIDi24255210.
KEGGictc:CTC_p60.
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.
PIRiA25689. BTCLTN.
RefSeqiWP_011100836.1. NC_004565.1.

3D structure databases

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

Chemistry databases

BindingDBiP04958.
ChEMBLiCHEMBL2036.
DrugBankiDB04465. Lactose.

Protein family/group databases

Allergomei2757. Clo t Toxoid.
MEROPSiM27.001.
TCDBi1.C.8.1.2. the botulinum and tetanus toxin (btt) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO37454; AAO37454; CTC_p60.
GeneIDi24255210.
KEGGictc:CTC_p60.
PATRICi19513592. VBICloTet101274_2814.

Phylogenomic databases

KOiK08644.
OMAiDFWGNPL.
OrthoDBiPOG091H19UB.

Enzyme and pathway databases

BRENDAi3.4.24.68. 1526.
ReactomeiR-HSA-5250982. Toxicity of tetanus toxin (TeNT).

Miscellaneous databases

EvolutionaryTraceiP04958.
PMAP-CutDBP04958.
PROiP04958.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
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]
ProtoNetiSearch...

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 2, 2016
This is version 151 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.