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P0A0L2 (ETXA_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Enterotoxin type A
Alternative name(s):
SEA
Gene names
Name:entA
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Cofactor

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

Subunit structure

Monomer.

Subcellular location

Secreted.

Miscellaneous

This toxin seems to be coded by a bacteriophage.

Sequence similarities

Belongs to the staphylococcal/streptococcal toxin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionEnterotoxin
Superantigen
Toxin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.2
Chain25 – 257233Enterotoxin type A
PRO_0000035604

Sites

Metal binding2111Zinc
Metal binding2491Zinc
Metal binding2511Zinc

Amino acid modifications

Disulfide bond120 ↔ 130

Experimental info

Sequence conflict2421T → S AA sequence Ref.2

Secondary structure

1 ......................................................... 257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A0L2 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: ADEBF5BCA1F14677

FASTA25729,669
        10         20         30         40         50         60 
MKKTAFTLLL FIALTLTTSP LVNGSEKSEE INEKDLRKKS ELQGTALGNL KQIYYYNEKA 

        70         80         90        100        110        120 
KTENKESHDQ FLQHTILFKG FFTDHSWYND LLVDFDSKDI VDKYKGKKVD LYGAYYGYQC 

       130        140        150        160        170        180 
AGGTPNKTAC MYGGVTLHDN NRLTEEKKVP INLWLDGKQN TVPLETVKTN KKNVTVQELD 

       190        200        210        220        230        240 
LQARRYLQEK YNLYNSDVFD GKVQRGLIVF HTSTEPSVNY DLFGAQGQYS NTLLRIYRDN 

       250 
KTINSENMHI DIYLYTS

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M18970 Genomic DNA. Translation: AAA26681.1.
PIRA28664.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0A0L2.
SMRP0A0L2. Positions 34-257.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-58974N.

Protein family/group databases

Allergome2139. Sta a SEA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.20.120. 1 hit.
InterProIPR008992. Enterotoxin_bac.
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]
PfamPF02876. Stap_Strp_tox_C. 1 hit.
PF01123. Stap_Strp_toxin. 1 hit.
[Graphical view]
PRINTSPR00279. BACTRLTOXIN.
PR01898. SAGSUPRFAMLY.
SUPFAMSSF50203. Bact_endotox. 1 hit.
SSF54334. Stap/Strep_toxin. 1 hit.
PROSITEPS00277. STAPH_STREP_TOXIN_1. 1 hit.
PS00278. STAPH_STREP_TOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A0L2.

Entry information

Entry nameETXA_STAAU
AccessionPrimary (citable) accession number: P0A0L2
Secondary accession number(s): P13163
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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