ID   ETXH_STAAW              Reviewed;         241 AA.
AC   P0A0L9; Q53585;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Enterotoxin type H;
DE   AltName: Full=SEH;
DE   Flags: Precursor;
GN   Name=entH; Synonyms=seh; OrderedLocusNames=MW0051;
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 via their
CC       alpha domain, in particular TRAV27. In turn, this ternary complex
CC       activates a large number of T-lymphocytes initiating a systemic release
CC       of pro-inflammatory cytokines. Causes also the intoxication
CC       staphylococcal food poisoning syndrome. The illness characterized by
CC       high fever, hypotension, diarrhea, shock, and in some cases death.
CC       {ECO:0000250|UniProtKB:P0A0M0}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P0A0M0};
CC       Note=Binds 1 zinc ion per subunit. The zinc ion is necessary for
CC       interaction with host MHC class II molecules.
CC       {ECO:0000250|UniProtKB:P0A0M0};
CC   -!- SUBUNIT: Interacts with host MHC class II molecules composed of
CC       alpha/HLA-DRA and beta/HLA-DRB1 chains. Interacts with host TCR alpha-
CC       chain TRAV27. {ECO:0000250|UniProtKB:P0A0M0}.
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; BAB93916.1; -; Genomic_DNA.
DR   RefSeq; WP_000608674.1; NC_003923.1.
DR   AlphaFoldDB; P0A0L9; -.
DR   SMR; P0A0L9; -.
DR   EnsemblBacteria; BAB93916; BAB93916; BAB93916.
DR   KEGG; sam:MW0051; -.
DR   HOGENOM; CLU_093855_0_0_9; -.
DR   OMA; AQEACEC; -.
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; 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..241
FT                   /note="Enterotoxin type H"
FT                   /id="PRO_0000035618"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   DISULFID        106..116
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   241 AA;  27859 MW;  70F77985877616CE CRC64;
     MINKIKILFS FLALLLSFTS YAKAEDLHDK SELTDLALAN AYGQYNHPFI KENIKSDEIS
     GEKDLIFRNQ GDSGNDLRVK FATADLAQKF KNKNVDIYGA SFYYKCEKIS ENISECLYGG
     TTLNSEKLAQ ERVIGANVWV DGIQKETELI RTNKKNVTLQ ELDIKIRKIL SDKYKIYYKD
     SEISKGLIEF DMKTPRDYSF DIYDLKGEND YEIDKIYEDN KTLKSDDISH IDVNLYTKKK
     V