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Protein

Enterotoxin type A

Gene

entA

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness is characterized by high fever, hypotension, diarrhea, shock, and in some cases death.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit. The zinc ion is necessary for the toxin interaction with MHC class II.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi211 – 2111Zinc
Metal bindingi249 – 2491Zinc
Metal bindingi251 – 2511Zinc

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. MHC class II protein binding Source: BHF-UCL

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Enterotoxin, Superantigen, Toxin

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Enterotoxin type A
Alternative name(s):
SEA
Gene namesi
Name:entA
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei2139. Sta a SEA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 257233Enterotoxin type APRO_0000035604Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi120 ↔ 130

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

DIPiDIP-58974N.

Structurei

Secondary structure

1
257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 314Combined sources
Helixi33 – 353Combined sources
Helixi39 – 413Combined sources
Helixi46 – 5510Combined sources
Beta strandi59 – 657Combined sources
Beta strandi72 – 787Combined sources
Beta strandi84 – 874Combined sources
Beta strandi89 – 946Combined sources
Helixi98 – 1047Combined sources
Beta strandi109 – 1146Combined sources
Helixi117 – 1193Combined sources
Beta strandi122 – 1243Combined sources
Helixi125 – 1273Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi135 – 1373Combined sources
Turni139 – 1413Combined sources
Beta strandi142 – 1487Combined sources
Beta strandi151 – 1555Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi166 – 17510Combined sources
Helixi176 – 19116Combined sources
Beta strandi193 – 1953Combined sources
Helixi197 – 1993Combined sources
Beta strandi205 – 2117Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi218 – 2214Combined sources
Beta strandi227 – 2293Combined sources
Turni230 – 2323Combined sources
Helixi233 – 2375Combined sources
Beta strandi242 – 2443Combined sources
Beta strandi249 – 2557Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYQX-ray1.50A25-257[»]
1ESFX-ray1.90A/B25-257[»]
1I4GX-ray2.10A/B25-257[»]
1I4HX-ray2.90A/B25-257[»]
1LO5X-ray3.20D25-257[»]
1SEAmodel-A25-257[»]
1SXTX-ray2.70A/B25-257[»]
ProteinModelPortaliP0A0L2.
SMRiP0A0L2. Positions 34-257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A0L2.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.20.120. 1 hit.
InterProiIPR008992. Enterotoxin.
IPR006126. Staph/Strept_toxin_CS.
IPR006173. Staph_tox_OB.
IPR016091. SuperAg_toxin_C.
IPR013307. Superantigen_bac.
IPR006123. Toxin_b-grasp_Staph/Strep.
IPR006177. Toxin_bac.
[Graphical view]
PfamiPF02876. Stap_Strp_tox_C. 1 hit.
PF01123. Stap_Strp_toxin. 1 hit.
[Graphical view]
PRINTSiPR00279. BACTRLTOXIN.
PR01898. SAGSUPRFAMLY.
SUPFAMiSSF50203. SSF50203. 1 hit.
SSF54334. SSF54334. 1 hit.
PROSITEiPS00277. STAPH_STREP_TOXIN_1. 1 hit.
PS00278. STAPH_STREP_TOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A0L2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKTAFTLLL FIALTLTTSP LVNGSEKSEE INEKDLRKKS ELQGTALGNL
60 70 80 90 100
KQIYYYNEKA KTENKESHDQ FLQHTILFKG FFTDHSWYND LLVDFDSKDI
110 120 130 140 150
VDKYKGKKVD LYGAYYGYQC AGGTPNKTAC MYGGVTLHDN NRLTEEKKVP
160 170 180 190 200
INLWLDGKQN TVPLETVKTN KKNVTVQELD LQARRYLQEK YNLYNSDVFD
210 220 230 240 250
GKVQRGLIVF HTSTEPSVNY DLFGAQGQYS NTLLRIYRDN KTINSENMHI

DIYLYTS
Length:257
Mass (Da):29,669
Last modified:February 15, 2005 - v1
Checksum:iADEBF5BCA1F14677
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421T → S AA sequence (PubMed:3584106)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18970 Genomic DNA. Translation: AAA26681.1.
PIRiA28664.
RefSeqiWP_000750412.1. NZ_JQIZ01000010.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18970 Genomic DNA. Translation: AAA26681.1.
PIRiA28664.
RefSeqiWP_000750412.1. NZ_JQIZ01000010.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYQX-ray1.50A25-257[»]
1ESFX-ray1.90A/B25-257[»]
1I4GX-ray2.10A/B25-257[»]
1I4HX-ray2.90A/B25-257[»]
1LO5X-ray3.20D25-257[»]
1SEAmodel-A25-257[»]
1SXTX-ray2.70A/B25-257[»]
ProteinModelPortaliP0A0L2.
SMRiP0A0L2. Positions 34-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58974N.

Protein family/group databases

Allergomei2139. Sta a SEA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP0A0L2.
PROiP0A0L2.

Family and domain databases

Gene3Di3.10.20.120. 1 hit.
InterProiIPR008992. Enterotoxin.
IPR006126. Staph/Strept_toxin_CS.
IPR006173. Staph_tox_OB.
IPR016091. SuperAg_toxin_C.
IPR013307. Superantigen_bac.
IPR006123. Toxin_b-grasp_Staph/Strep.
IPR006177. Toxin_bac.
[Graphical view]
PfamiPF02876. Stap_Strp_tox_C. 1 hit.
PF01123. Stap_Strp_toxin. 1 hit.
[Graphical view]
PRINTSiPR00279. BACTRLTOXIN.
PR01898. SAGSUPRFAMLY.
SUPFAMiSSF50203. SSF50203. 1 hit.
SSF54334. SSF54334. 1 hit.
PROSITEiPS00277. STAPH_STREP_TOXIN_1. 1 hit.
PS00278. STAPH_STREP_TOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the type A staphylococcal enterotoxin gene."
    Betley M.J., Mekalanos J.J.
    J. Bacteriol. 170:34-41(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: FRI337.
  2. "Complete amino acid sequence of staphylococcal enterotoxin A."
    Huang I.-Y., Hughes J.L., Bergdoll M.S., Schantz E.J.
    J. Biol. Chem. 262:7006-7013(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-257.
  3. "Crystal structure of the superantigen staphylococcal enterotoxin type A."
    Schad E.M., Zaitseva I., Zaitsev V.N., Dohlsten M., Kalland T., Schlievert P.M., Ohlendorf D.H., Svensson L.A.
    EMBO J. 14:3292-3301(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  4. "The Co-crystal structure of staphylococcal enterotoxin type A with Zn2+ at 2.7-A resolution. Implications for major histocompatibility complex class II binding."
    Sundstroem M., Hallen D., Svensson A., Schad E., Dohlsten M., Abrahmsen L.
    J. Biol. Chem. 271:32212-32216(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  5. "Residues defining V beta specificity in staphylococcal enterotoxins."
    Swaminathan S., Furey W.F. Jr., Pletcher J., Sax M.
    Nat. Struct. Biol. 2:680-686(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  6. "A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity."
    Schad E.M., Papageorgiou A.C., Svensson L.A., Acharya K.R.
    J. Mol. Biol. 269:270-280(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPARISON OF STRUCTURE OF SEA AND SEC2.

Entry informationi

Entry nameiETXA_STAAU
AccessioniPrimary (citable) accession number: P0A0L2
Secondary accession number(s): P13163
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: January 7, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This toxin seems to be coded by a bacteriophage.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.