ID   ETXG_STAAU              Reviewed;         258 AA.
AC   P0A0L8; O85382; Q52T98;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Enterotoxin type G;
DE   AltName: Full=SEG;
DE   Flags: Precursor;
GN   Name=entG; Synonyms=seg;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=FRI572;
RX   PubMed=9632603; DOI=10.1128/iai.66.7.3337-3348.1998;
RA   Munson S.H., Tremaine M.T., Betley M.J., Welch R.A.;
RT   "Identification and characterization of staphylococcal enterotoxin types G
RT   and I from Staphylococcus aureus.";
RL   Infect. Immun. 66:3337-3348(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-258, X-RAY CRYSTALLOGRAPHY (1.9
RP   ANGSTROMS) OF 26-258, AND DISULFIDE BOND.
RC   STRAIN=Fc30, Fc35, and Fc65;
RX   PubMed=17427250; DOI=10.1002/prot.21388;
RA   Fernandez M.M., Bhattacharya S., De Marzi M.C., Brown P.H., Kerzic M.,
RA   Schuck P., Mariuzza R.A., Malchiodi E.L.;
RT   "Superantigen natural affinity maturation revealed by the crystal structure
RT   of staphylococcal enterotoxin G and its binding to T-cell receptor
RT   Vbeta8.2.";
RL   Proteins 68:389-402(2007).
CC   -!- FUNCTION: Staphylococcal enterotoxins cause the intoxication
CC       staphylococcal food poisoning syndrome. The illness is characterized by
CC       high fever, hypotension, diarrhea, shock, and in some cases death.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC       {ECO:0000305}.
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DR   EMBL; AF064773; AAC26660.1; -; Genomic_DNA.
DR   EMBL; AY961383; AAX84812.1; -; Genomic_DNA.
DR   EMBL; AY961384; AAX84813.1; -; Genomic_DNA.
DR   EMBL; AY961386; AAX84815.1; -; Genomic_DNA.
DR   RefSeq; WP_000736712.1; NZ_WYDB01000002.1.
DR   PDB; 1XXG; X-ray; 2.20 A; A=26-258.
DR   PDBsum; 1XXG; -.
DR   AlphaFoldDB; P0A0L8; -.
DR   SMR; P0A0L8; -.
DR   EvolutionaryTrace; P0A0L8; -.
DR   PRO; PR:P0A0L8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Enterotoxin;
KW   Secreted; Signal; Superantigen; Toxin; Virulence.
FT   SIGNAL          1..25
FT   CHAIN           26..258
FT                   /note="Enterotoxin type G"
FT                   /id="PRO_0000035616"
FT   DISULFID        116..133
FT                   /evidence="ECO:0000269|PubMed:17427250"
FT   HELIX           31..33
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   HELIX           37..42
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   HELIX           48..55
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   HELIX           94..100
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          149..157
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   TURN            158..160
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          161..170
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          172..175
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   HELIX           176..191
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          200..209
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          215..221
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   HELIX           231..233
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   HELIX           235..238
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          243..245
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:1XXG"
FT   STRAND          250..256
FT                   /evidence="ECO:0007829|PDB:1XXG"
SQ   SEQUENCE   258 AA;  29940 MW;  E2982101701D012C CRC64;
     MKKLSTVIII LILEIVFHNM NYVNAQPDPK LDELNKVSDY KNNKGTMGNV MNLYTSPPVE
     GRGVINSRQF LSHDLIFPIE YKSYNEVKTE LENTELANNY KDKKVDIFGV PYFYTCIIPK
     SEPDINQNFG GCCMYGGLTF NSSENERDKL ITVQVTIDNR QSLGFTITTN KNMVTIQELD
     YKARHWLTKE KKLYEFDGSA FESGYIKFTE KNNTSFWFDL FPKKELVPFV PYKFLNIYGD
     NKVVDSKSIK MEVFLNTH