ETXE_STAAU
ID ETXE_STAAU Reviewed; 257 AA.
AC P12993;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Enterotoxin type E;
DE AltName: Full=SEE;
DE Flags: Precursor;
GN Name=entE;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-74.
RC STRAIN=MJB265;
RX PubMed=3384800; DOI=10.1128/jb.170.7.2954-2960.1988;
RA Couch J.L., Soltis M.T., Betley M.J.;
RT "Cloning and nucleotide sequence of the type E staphylococcal enterotoxin
RT gene.";
RL J. Bacteriol. 170:2954-2960(1988).
RN [2]
RP 3D-STRUCTURE MODELING.
RX PubMed=7552730; DOI=10.1038/nsb0895-680;
RA Swaminathan S., Furey W.F. Jr., Pletcher J., Sax M.;
RT "Residues defining V beta specificity in staphylococcal enterotoxins.";
RL Nat. Struct. Biol. 2:680-686(1995).
RN [3]
RP FUNCTION.
RX PubMed=20394711;
RA Ostyn A., De Buyser M.L., Guillier F., Groult J., Felix B., Salah S.,
RA Delmas G., Hennekinne J.A.;
RT "First evidence of a food poisoning outbreak due to staphylococcal
RT enterotoxin type E, France, 2009.";
RL Eurosurveillance 15:880-885(2010).
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST TRBV7-9; HLA-DRA AND HLA-DRB1.
RX PubMed=24194959; DOI=10.1371/journal.pone.0079082;
RA Hedlund G., Eriksson H., Sundstedt A., Forsberg G., Jakobsen B.K.,
RA Pumphrey N., Roedstroem K., Lindkvist-Petersson K., Bjoerk P.;
RT "The tumor targeted superantigen ABR-217620 selectively engages TRBV7-9 and
RT exploits TCR-pMHC affinity mimicry in mediating T cell cytotoxicity.";
RL PLoS ONE 8:E79082-E79082(2013).
RN [5] {ECO:0007744|PDB:4UDU}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 25-257 IN COMPLEX WITH ZINC,
RP DISULFIDE BONDS, AND INTERACTION WITH HOST TRBV7-9.
RX PubMed=26147596; DOI=10.1371/journal.pone.0131988;
RA Rodstrom K.E., Regenthal P., Lindkvist-Petersson K.;
RT "Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the
RT Role of TCR Loop Positioning in Superantigen Recognition.";
RL PLoS ONE 10:e0131988-e0131988(2015).
RN [6] {ECO:0007744|PDB:5FKA}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 25-257 IN COMPLEX WITH ZINC,
RP DISULFIDE BONDS, AND INTERACTION WITH HOST TRBV7-9.
RX PubMed=27180909; DOI=10.1038/srep25796;
RA Rodstrom K.E., Regenthal P., Bahl C., Ford A., Baker D.,
RA Lindkvist-Petersson K.;
RT "Two common structural motifs for TCR recognition by staphylococcal
RT enterotoxins.";
RL Sci. Rep. 6:25796-25796(2016).
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 this ternary complex activates a large number of T-lymphocytes
CC initiating a systemic release of pro-inflammatory cytokines
CC (PubMed:24194959). Causes also the intoxication staphylococcal food
CC poisoning syndrome (PubMed:20394711). {ECO:0000269|PubMed:20394711,
CC ECO:0000269|PubMed:24194959}.
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: Interacts with host MHC class II molecules composed of
CC alpha/HLA-DRA and beta/HLA-DRB1 chains (PubMed:24194959). Interacts
CC with host T-cell receptor beta variable TRBV7-9 (PubMed:24194959,
CC PubMed:26147596, PubMed:27180909). {ECO:0000269|PubMed:24194959,
CC ECO:0000269|PubMed:26147596, ECO:0000269|PubMed:27180909}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC {ECO:0000305}.
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DR EMBL; M21319; AAA26617.1; -; Genomic_DNA.
DR PIR; A28179; A28179.
DR PDB; 4UDU; X-ray; 2.50 A; C=25-257.
DR PDB; 5FKA; X-ray; 2.40 A; C=25-257.
DR PDBsum; 4UDU; -.
DR PDBsum; 5FKA; -.
DR AlphaFoldDB; P12993; -.
DR SMR; P12993; -.
DR Allergome; 2428; Sta a SEE.
DR PRIDE; P12993; -.
DR PRO; PR:P12993; -.
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 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..27
FT /evidence="ECO:0000269|PubMed:3384800"
FT CHAIN 28..257
FT /note="Enterotoxin type E"
FT /id="PRO_0000035613"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:26147596,
FT ECO:0000269|PubMed:27180909, ECO:0007744|PDB:4UDU,
FT ECO:0007744|PDB:5FKA"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:26147596,
FT ECO:0000269|PubMed:27180909, ECO:0007744|PDB:4UDU,
FT ECO:0007744|PDB:5FKA"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:26147596,
FT ECO:0000269|PubMed:27180909, ECO:0007744|PDB:4UDU,
FT ECO:0007744|PDB:5FKA"
FT DISULFID 120..130
FT /evidence="ECO:0000269|PubMed:26147596,
FT ECO:0000269|PubMed:27180909, ECO:0007744|PDB:4UDU,
FT ECO:0007744|PDB:5FKA"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:5FKA"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:5FKA"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:5FKA"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4UDU"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:5FKA"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:5FKA"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:4UDU"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5FKA"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:5FKA"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:5FKA"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:5FKA"
SQ SEQUENCE 257 AA; 29358 MW; 27EDA94B97770CE3 CRC64;
MKKTAFILLL FIALTLTTSP LVNGSEKSEE INEKDLRKKS ELQRNALSNL RQIYYYNEKA
ITENKESDDQ FLENTLLFKG FFTGHPWYND LLVDLGSKDA TNKYKGKKVD LYGAYYGYQC
AGGTPNKTAC MYGGVTLHDN NRLTEEKKVP INLWIDGKQT TVPIDKVKTS KKEVTVQELD
LQARHYLHGK FGLYNSDSFG GKVQRGLIVF HSSEGSTVSY DLFDAQGQYP DTLLRIYRDN
KTINSENLHI DLYLYTT
