ID   ETXA_STAAW              Reviewed;         257 AA.
AC   P0A0L1; P13163;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Enterotoxin type A;
DE   AltName: Full=SEA;
DE   Flags: Precursor;
GN   Name=entA; OrderedLocusNames=MW1889;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Staphylococcal enterotoxin that activates the host immune
CC       system by binding as unprocessed molecules to major histocompatibility
CC       (MHC) complex class II and T-cell receptor (TCR) molecules. In turn,
CC       waves of cellular activation, cytokine production, and migration into
CC       the lung tissue and airways occur via alphabeta T-cells. Causes also
CC       the intoxication staphylococcal food poisoning syndrome. The illness is
CC       characterized by high fever, hypotension, diarrhea, shock, and in some
CC       cases death. {ECO:0000250|UniProtKB:P0A0L2}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. The zinc ion is necessary for the
CC       toxin interaction with MHC class II. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. Interacts with MHC class II molecules alpha/HLA-DRB1
CC       and beta/HLA-DRA chains. The interaction with MHC-II molecules occurs
CC       at both zinc-dependent and zinc-independent sites. Interacts with T-
CC       cell receptor beta variable 7-9/TRBV7-9.
CC       {ECO:0000250|UniProtKB:P0A0L2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC       {ECO:0000305}.
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DR   EMBL; BA000033; BAB95754.1; -; Genomic_DNA.
DR   RefSeq; WP_000750412.1; NC_003923.1.
DR   AlphaFoldDB; P0A0L1; -.
DR   SMR; P0A0L1; -.
DR   Allergome; 2139; Sta a SEA.
DR   EnsemblBacteria; BAB95754; BAB95754; BAB95754.
DR   KEGG; sam:MW1889; -.
DR   HOGENOM; CLU_093855_0_0_9; -.
DR   OMA; NGNKHES; -.
DR   PRO; PR:P0A0L1; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR008992; Enterotoxin.
DR   InterPro; IPR006126; Staph/Strept_toxin_CS.
DR   InterPro; IPR006173; Staph_tox_OB.
DR   InterPro; IPR016091; SuperAg_toxin_C.
DR   InterPro; IPR013307; Superantigen_bac.
DR   InterPro; IPR006123; Toxin_b-grasp_Staph/Strep.
DR   InterPro; IPR006177; Toxin_bac.
DR   Pfam; PF02876; Stap_Strp_tox_C; 1.
DR   Pfam; PF01123; Stap_Strp_toxin; 1.
DR   PRINTS; PR00279; BACTRLTOXIN.
DR   PRINTS; PR01898; SAGSUPRFAMLY.
DR   SUPFAM; SSF50203; SSF50203; 1.
DR   SUPFAM; SSF54334; SSF54334; 1.
DR   PROSITE; PS00277; STAPH_STREP_TOXIN_1; 1.
DR   PROSITE; PS00278; STAPH_STREP_TOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Enterotoxin; Metal-binding; Secreted; Signal; Superantigen;
KW   Toxin; Virulence; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..257
FT                   /note="Enterotoxin type A"
FT                   /id="PRO_0000035605"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A0L2"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A0L2"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0A0L2"
FT   DISULFID        120..130
FT                   /evidence="ECO:0000250|UniProtKB:P0A0L2"
SQ   SEQUENCE   257 AA;  29669 MW;  ADEBF5BCA1F14677 CRC64;
     MKKTAFTLLL FIALTLTTSP LVNGSEKSEE INEKDLRKKS ELQGTALGNL KQIYYYNEKA
     KTENKESHDQ FLQHTILFKG FFTDHSWYND LLVDFDSKDI VDKYKGKKVD LYGAYYGYQC
     AGGTPNKTAC MYGGVTLHDN NRLTEEKKVP INLWLDGKQN TVPLETVKTN KKNVTVQELD
     LQARRYLQEK YNLYNSDVFD GKVQRGLIVF HTSTEPSVNY DLFGAQGQYS NTLLRIYRDN
     KTINSENMHI DIYLYTS