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ETXA_STAAU
ID   ETXA_STAAU              Reviewed;         257 AA.
AC   P0A0L2; P13163;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Enterotoxin type A;
DE   AltName: Full=SEA;
DE   Flags: Precursor;
GN   Name=entA;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FRI337;
RX   PubMed=3335483; DOI=10.1128/jb.170.1.34-41.1988;
RA   Betley M.J., Mekalanos J.J.;
RT   "Nucleotide sequence of the type A staphylococcal enterotoxin gene.";
RL   J. Bacteriol. 170:34-41(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-257.
RX   PubMed=3584106; DOI=10.1016/s0021-9258(18)48194-x;
RA   Huang I.-Y., Hughes J.L., Bergdoll M.S., Schantz E.J.;
RT   "Complete amino acid sequence of staphylococcal enterotoxin A.";
RL   J. Biol. Chem. 262:7006-7013(1987).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH MHC CLASS II ANTIGEN DR1/HLA-DRB1 AND
RP   HLA-DRA.
RX   PubMed=2658055; DOI=10.1126/science.2658055;
RA   Mollick J.A., Cook R.G., Rich R.R.;
RT   "Class II MHC molecules are specific receptors for staphylococcus
RT   enterotoxin A.";
RL   Science 244:817-820(1989).
RN   [4]
RP   REVIEW ON FUNCTION.
RX   PubMed=22069659; DOI=10.3390/toxins2071751;
RA   Argudin M.A., Mendoza M.C., Rodicio M.R.;
RT   "Food poisoning and Staphylococcus aureus enterotoxins.";
RL   Toxins 2:1751-1773(2010).
RN   [5]
RP   FUNCTION.
RX   PubMed=23321986; DOI=10.1038/mi.2012.138;
RA   Kumar S., Colpitts S.L., Menoret A., Budelsky A.L., Lefrancois L.,
RA   Vella A.T.;
RT   "Rapid alphabeta T-cell responses orchestrate innate immunity in response
RT   to Staphylococcal enterotoxin A.";
RL   Mucosal Immunol. 6:1006-1015(2013).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=7628431; DOI=10.1002/j.1460-2075.1995.tb07336.x;
RA   Schad E.M., Zaitseva I., Zaitsev V.N., Dohlsten M., Kalland T.,
RA   Schlievert P.M., Ohlendorf D.H., Svensson L.A.;
RT   "Crystal structure of the superantigen staphylococcal enterotoxin type A.";
RL   EMBO J. 14:3292-3301(1995).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ZINC.
RX   PubMed=8943278; DOI=10.1074/jbc.271.50.32212;
RA   Sundstroem M., Hallen D., Svensson A., Schad E., Dohlsten M., Abrahmsen L.;
RT   "The Co-crystal structure of staphylococcal enterotoxin type A with Zn2+ at
RT   2.7-A resolution. Implications for major histocompatibility complex class
RT   II binding.";
RL   J. Biol. Chem. 271:32212-32216(1996).
RN   [8]
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   [9]
RP   COMPARISON OF STRUCTURE OF SEA AND SEC2.
RX   PubMed=9191070; DOI=10.1006/jmbi.1997.1023;
RA   Schad E.M., Papageorgiou A.C., Svensson L.A., Acharya K.R.;
RT   "A structural and functional comparison of staphylococcal enterotoxins A
RT   and C2 reveals remarkable similarity and dissimilarity.";
RL   J. Mol. Biol. 269:270-280(1997).
RN   [10] {ECO:0007744|PDB:1I4G, ECO:0007744|PDB:1I4H}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ZINC, AND
RP   MUTAGENESIS OF HIS-211.
RX   PubMed=11713682; DOI=10.1007/s007750100251;
RA   Haakansson M., Antonsson P., Bjoerk P., Svensson L.A.;
RT   "Cooperative zinc binding in a staphylococcal enterotoxin A mutant mimics
RT   the SEA-MHC class II interaction.";
RL   J. Biol. Inorg. Chem. 6:757-762(2001).
RN   [11] {ECO:0007744|PDB:1DYQ}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC, AND
RP   INTERACTION WITH MHC CLASS II ANTIGEN DR1/HLA-DRB1 AND HLA-DRA.
RX   PubMed=11847286; DOI=10.1110/ps.39702;
RA   Krupka H.I., Segelke B.W., Ulrich R.G., Ringhofer S., Knapp M., Rupp B.;
RT   "Structural basis for abrogated binding between staphylococcal enterotoxin
RT   A superantigen vaccine and MHC-IIalpha.";
RL   Protein Sci. 11:642-651(2002).
RN   [12] {ECO:0007744|PDB:1LO5}
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), MUTAGENESIS OF ASP-251, INTERACTION
RP   WITH HOST HLA-DRA, AND FUNCTION.
RX   PubMed=12467569; DOI=10.1016/s0969-2126(02)00895-x;
RA   Petersson K., Thunnissen M., Forsberg G., Walse B.;
RT   "Crystal structure of a SEA variant in complex with MHC class II reveals
RT   the ability of SEA to crosslink MHC molecules.";
RL   Structure 10:1619-1626(2002).
RN   [13] {ECO:0007744|PDB:5FK9}
RP   X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS), FUNCTION, INTERACTION WITH HOST T
RP   CELL RECEPTOR BETA VARIABLE 7-9/TRBV7-9, AND DISULFIDE BOND.
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
CC       (PubMed:2658055, PubMed:12467569). In turn, waves of cellular
CC       activation, cytokine production, and migration into the lung tissue and
CC       airways occur via alphabeta T-cells (PubMed:23321986). Causes also the
CC       intoxication staphylococcal food poisoning syndrome. The illness is
CC       characterized by high fever, hypotension, diarrhea, shock, and in some
CC       cases death (Probable). {ECO:0000269|PubMed:12467569,
CC       ECO:0000269|PubMed:23321986, ECO:0000269|PubMed:2658055,
CC       ECO:0000305|PubMed:22069659}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit. The zinc ion is necessary for the
CC       toxin interaction with MHC class II.;
CC   -!- SUBUNIT: Monomer. Interacts with MHC class II molecules alpha/HLA-DRB1
CC       and beta/HLA-DRA chains (PubMed:2658055, PubMed:12467569,
CC       PubMed:11847286). The interaction with MHC-II molecules occurs at both
CC       zinc-dependent and zinc-independent sites (PubMed:2658055,
CC       PubMed:12467569). Interacts with T-cell receptor beta variable 7-
CC       9/TRBV7-9 (PubMed:27180909). {ECO:0000269|PubMed:11847286,
CC       ECO:0000269|PubMed:12467569, ECO:0000269|PubMed:2658055,
CC       ECO:0000269|PubMed:27180909}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: This toxin seems to be coded by a bacteriophage.
CC   -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC       {ECO:0000305}.
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DR   EMBL; M18970; AAA26681.1; -; Genomic_DNA.
DR   PIR; A28664; A28664.
DR   RefSeq; WP_000750412.1; NZ_WOFG01000001.1.
DR   PDB; 1DYQ; X-ray; 1.50 A; A=25-257.
DR   PDB; 1ESF; X-ray; 1.90 A; A/B=25-257.
DR   PDB; 1I4G; X-ray; 2.10 A; A/B=25-257.
DR   PDB; 1I4H; X-ray; 2.90 A; A/B=25-257.
DR   PDB; 1LO5; X-ray; 3.20 A; D=25-257.
DR   PDB; 1SXT; X-ray; 2.70 A; A/B=25-257.
DR   PDB; 5FK9; X-ray; 3.10 A; C=25-257.
DR   PDBsum; 1DYQ; -.
DR   PDBsum; 1ESF; -.
DR   PDBsum; 1I4G; -.
DR   PDBsum; 1I4H; -.
DR   PDBsum; 1LO5; -.
DR   PDBsum; 1SXT; -.
DR   PDBsum; 5FK9; -.
DR   AlphaFoldDB; P0A0L2; -.
DR   SMR; P0A0L2; -.
DR   DIP; DIP-58974N; -.
DR   IntAct; P0A0L2; 1.
DR   Allergome; 2139; Sta a SEA.
DR   OMA; NGNKHES; -.
DR   EvolutionaryTrace; P0A0L2; -.
DR   PRO; PR:P0A0L2; -.
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:BHF-UCL.
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; 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; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:3584106"
FT   CHAIN           25..257
FT                   /note="Enterotoxin type A"
FT                   /id="PRO_0000035604"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:11847286,
FT                   ECO:0007744|PDB:1DYQ"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:11713682,
FT                   ECO:0000269|PubMed:11847286, ECO:0007744|PDB:1DYQ,
FT                   ECO:0007744|PDB:1I4G, ECO:0007744|PDB:1I4H"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:11713682,
FT                   ECO:0000269|PubMed:11847286, ECO:0007744|PDB:1DYQ,
FT                   ECO:0007744|PDB:1I4G, ECO:0007744|PDB:1I4H"
FT   DISULFID        120..130
FT                   /evidence="ECO:0000269|PubMed:27180909,
FT                   ECO:0007744|PDB:5FK9"
FT   MUTAGEN         211
FT                   /note="H->A: Almost 10-fold reduction of the binding to
FT                   major histocompatibility complex (MHC) class II."
FT                   /evidence="ECO:0000269|PubMed:11713682"
FT   MUTAGEN         251
FT                   /note="D->A: Loss of interaction with the beta chain of
FT                   HLA-DR1 through the zinc-dependent site."
FT                   /evidence="ECO:0000269|PubMed:12467569"
FT   CONFLICT        242
FT                   /note="T -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           28..31
FT                   /evidence="ECO:0007829|PDB:1ESF"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:5FK9"
FT   HELIX           46..55
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          59..65
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          72..78
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:1SXT"
FT   STRAND          89..94
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   HELIX           98..104
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          109..114
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:1ESF"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:1SXT"
FT   STRAND          128..133
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:1SXT"
FT   STRAND          142..148
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          151..155
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          166..175
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   HELIX           176..191
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:5FK9"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          205..211
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          218..221
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:1ESF"
FT   TURN            230..232
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   HELIX           233..237
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          242..244
FT                   /evidence="ECO:0007829|PDB:1DYQ"
FT   STRAND          249..255
FT                   /evidence="ECO:0007829|PDB:1DYQ"
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
 
 
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