ETXH_STAAU
ID ETXH_STAAU Reviewed; 241 AA.
AC P0A0M0; Q53585;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Enterotoxin type H;
DE AltName: Full=SEH;
DE Flags: Precursor;
GN Name=entH; Synonyms=seh;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RC STRAIN=D4508;
RX PubMed=7964453; DOI=10.1084/jem.180.5.1675;
RA Ren K., Bannan J.D., Pancholi V., Cheung A.L., Robbins J.C.,
RA Fischetti V.A., Zabriskie J.B.;
RT "Characterization and biological properties of a new staphylococcal
RT exotoxin.";
RL J. Exp. Med. 180:1675-1683(1994).
RN [2]
RP FUNCTION, INTERACTION WITH HOST HLA-DRB1, AND MUTAGENESIS OF ASP-191;
RP ASP-227 AND ASP-232.
RX PubMed=10586065;
RA Nilsson H., Bjoerk P., Dohlsten M., Antonsson P.;
RT "Staphylococcal enterotoxin H displays unique MHC class II-binding
RT properties.";
RL J. Immunol. 163:6686-6693(1999).
RN [3]
RP FUNCTION.
RX PubMed=12682246; DOI=10.4049/jimmunol.170.8.4148;
RA Petersson K., Pettersson H., Skartved N.J., Walse B., Forsberg G.;
RT "Staphylococcal enterotoxin H induces V alpha-specific expansion of T
RT cells.";
RL J. Immunol. 170:4148-4154(2003).
RN [4]
RP FUNCTION.
RX PubMed=16213675; DOI=10.1016/j.femsle.2005.09.005;
RA Joergensen H.J., Mathisen T., Loevseth A., Omoe K., Qvale K.S.,
RA Loncarevic S.;
RT "An outbreak of staphylococcal food poisoning caused by enterotoxin H in
RT mashed potato made with raw milk.";
RL FEMS Microbiol. Lett. 252:267-272(2005).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST TRAV27.
RX PubMed=17709482; DOI=10.4049/jimmunol.179.5.2700;
RA Pumphrey N., Vuidepot A., Jakobsen B., Forsberg G., Walse B.,
RA Lindkvist-Petersson K.;
RT "Cutting edge: Evidence of direct TCR alpha-chain interaction with
RT superantigen.";
RL J. Immunol. 179:2700-2704(2007).
RN [6] {ECO:0007744|PDB:1ENF, ECO:0007744|PDB:1EWC, ECO:0007744|PDB:1F77}
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 26-237 IN COMPLEX WITH ZINC, AND
RP DISULFIDE BONDS.
RX PubMed=10986116; DOI=10.1006/jmbi.2000.4093;
RA Hakansson M., Petersson K., Nilsson H., Forsberg G., Bjork P.,
RA Antonsson P., Svensson L.A.;
RT "The crystal structure of staphylococcal enterotoxin H: implications for
RT binding properties to MHC class II and TcR molecules.";
RL J. Mol. Biol. 302:527-537(2000).
RN [7] {ECO:0007744|PDB:1HXY}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-237 IN COMPLEX WITH ZINC,
RP DISULFIDE BONDS, AND INTERACTION WITH HOST HLA-DRA AND HLA-DRB1.
RX PubMed=11432818; DOI=10.1093/emboj/20.13.3306;
RA Petersson K., Haakansson M., Nilsson H., Forsberg G., Svensson L.A.,
RA Liljas A., Walse B.;
RT "Crystal structure of a superantigen bound to MHC class II displays zinc
RT and peptide dependence.";
RL EMBO J. 20:3306-3312(2001).
RN [8] {ECO:0007744|PDB:2XN9, ECO:0007744|PDB:2XNA}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 25-241, DISULFIDE BONDS,
RP FUNCTION, AND INTERACTION WITH HOST TRAV27; HLA-DRA AND HLA-DRB1.
RX PubMed=21081917; DOI=10.1038/ncomms1117;
RA Saline M., Roedstroem K.E., Fischer G., Orekhov V.Y., Karlsson B.G.,
RA Lindkvist-Petersson K.;
RT "The structure of superantigen complexed with TCR and MHC reveals novel
RT insights into superantigenic T cell activation.";
RL Nat. Commun. 1:119-119(2010).
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 (PubMed:12682246, PubMed:17709482,
CC PubMed:21081917). In turn, this ternary complex activates a large
CC number of T-lymphocytes initiating a systemic release of pro-
CC inflammatory cytokines (PubMed:12682246, PubMed:10586065). Causes also
CC the intoxication staphylococcal food poisoning syndrome. The illness
CC characterized by high fever, hypotension, diarrhea, shock, and in some
CC cases death (PubMed:16213675). {ECO:0000269|PubMed:10586065,
CC ECO:0000269|PubMed:12682246, ECO:0000269|PubMed:16213675,
CC ECO:0000269|PubMed:17709482, ECO:0000269|PubMed:21081917}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit. The zinc ion is necessary for
CC interaction with host MHC class II molecules.
CC {ECO:0000269|PubMed:10586065, ECO:0000269|PubMed:11432818};
CC -!- SUBUNIT: Interacts with host MHC class II molecules composed of
CC alpha/HLA-DRA and beta/HLA-DRB1 chains (PubMed:11432818,
CC PubMed:21081917, PubMed:10586065). Interacts with host TCR alpha-chain
CC TRAV27 (PubMed:17709482, PubMed:21081917).
CC {ECO:0000269|PubMed:10586065, ECO:0000269|PubMed:11432818,
CC ECO:0000269|PubMed:17709482, ECO:0000269|PubMed:21081917}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC {ECO:0000305}.
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DR EMBL; U11702; AAA19777.1; -; Genomic_DNA.
DR RefSeq; WP_000608674.1; NZ_WJSW01000002.1.
DR PDB; 1ENF; X-ray; 1.69 A; A=26-237.
DR PDB; 1EWC; X-ray; 1.95 A; A=26-239.
DR PDB; 1F77; X-ray; 2.40 A; A/B=25-241.
DR PDB; 1HXY; X-ray; 2.60 A; D=25-237.
DR PDB; 2XN9; X-ray; 2.30 A; C=25-241.
DR PDB; 2XNA; X-ray; 2.10 A; C=25-241.
DR PDBsum; 1ENF; -.
DR PDBsum; 1EWC; -.
DR PDBsum; 1F77; -.
DR PDBsum; 1HXY; -.
DR PDBsum; 2XN9; -.
DR PDBsum; 2XNA; -.
DR AlphaFoldDB; P0A0M0; -.
DR SMR; P0A0M0; -.
DR PRIDE; P0A0M0; -.
DR OMA; AQEACEC; -.
DR EvolutionaryTrace; P0A0M0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042289; F:MHC class II protein binding; IPI:UniProtKB.
DR GO; GO:0042608; F:T cell receptor binding; IPI:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Enterotoxin;
KW Metal-binding; Secreted; Signal; Superantigen; Toxin; Virulence; Zinc.
FT SIGNAL 1..24
FT CHAIN 25..241
FT /note="Enterotoxin type H"
FT /id="PRO_0000035617"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:10986116"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:10986116,
FT ECO:0000269|PubMed:11432818, ECO:0007744|PDB:1EWC,
FT ECO:0007744|PDB:1HXY"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:11432818,
FT ECO:0007744|PDB:1EWC, ECO:0007744|PDB:1HXY"
FT DISULFID 106..116
FT /evidence="ECO:0000269|PubMed:10986116,
FT ECO:0000269|PubMed:11432818, ECO:0000269|PubMed:21081917,
FT ECO:0007744|PDB:1ENF, ECO:0007744|PDB:1EWC,
FT ECO:0007744|PDB:1F77, ECO:0007744|PDB:1HXY,
FT ECO:0007744|PDB:2XN9, ECO:0007744|PDB:2XNA"
FT MUTAGEN 191
FT /note="D->A: About 35-fold reduction in host MHC class II
FT binding."
FT /evidence="ECO:0000269|PubMed:10586065"
FT MUTAGEN 227
FT /note="D->A: About 22-fold reduction in host MHC class II
FT binding."
FT /evidence="ECO:0000269|PubMed:10586065"
FT MUTAGEN 232
FT /note="D->A: About 5000-fold reduction in host MHC class II
FT binding."
FT /evidence="ECO:0000269|PubMed:10586065"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1ENF"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1ENF"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1ENF"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1ENF"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 127..140
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:1ENF"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:1ENF"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:1ENF"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1ENF"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1ENF"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:1ENF"
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
