ID   SPEA_STRPY              Reviewed;         250 AA.
AC   P0DJY7; P08095; P62560;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Exotoxin type A;
DE   AltName: Full=Erythrogenic toxin;
DE   AltName: Full=SPE A;
DE   AltName: Full=Scarlet fever toxin;
DE   Flags: Precursor;
GN   Name=speA;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3526093; DOI=10.1007/bf00333979;
RA   Johnson L.P., L'Italien J.J., Schlievert P.M.;
RT   "Streptococcal pyrogenic exotoxin type A (scarlet fever toxin) is related
RT   to Staphylococcus aureus enterotoxin B.";
RL   Mol. Gen. Genet. 203:354-356(1986).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 33-250.
RX   PubMed=9878045; DOI=10.1093/emboj/18.1.9;
RA   Papageorgiou A.C., Collins C.M., Gutman D.M., Kline J.B., O'Brien S.M.,
RA   Tranter H.S., Acharya K.R.;
RT   "Structural basis for the recognition of superantigen streptococcal
RT   pyrogenic exotoxin A (SpeA1) by MHC class II molecules and T-cell
RT   receptors.";
RL   EMBO J. 18:9-21(1999).
CC   -!- FUNCTION: Causative agent of the symptoms associated with scarlet
CC       fever, have been associated with streptococcal toxic shock-like disease
CC       and may play a role in the early events of rheumatic fever.
CC   -!- MISCELLANEOUS: Binds to major histocompatibility complex class II beta
CC       chain.
CC   -!- MISCELLANEOUS: This toxin is coded by bacteriophage T12.
CC   -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC       {ECO:0000305}.
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DR   EMBL; X03929; CAA27568.1; -; Genomic_DNA.
DR   PIR; A26152; A26152.
DR   PDB; 1B1Z; X-ray; 2.57 A; A/B/C/D=60-250.
DR   PDB; 1FNU; X-ray; 1.94 A; A/B/C/D=60-250.
DR   PDB; 1FNV; X-ray; 3.60 A; A/B/C/D=60-250.
DR   PDB; 1FNW; X-ray; 3.90 A; A/B/C/D/E/F/G/H=60-250.
DR   PDB; 1HA5; X-ray; 2.82 A; A/B/C/D=60-249.
DR   PDB; 1L0X; X-ray; 2.80 A; B/D=60-250.
DR   PDB; 1L0Y; X-ray; 2.50 A; B/D=60-250.
DR   PDB; 1UUP; X-ray; 2.60 A; A/B/C/D=60-250.
DR   PDBsum; 1B1Z; -.
DR   PDBsum; 1FNU; -.
DR   PDBsum; 1FNV; -.
DR   PDBsum; 1FNW; -.
DR   PDBsum; 1HA5; -.
DR   PDBsum; 1L0X; -.
DR   PDBsum; 1L0Y; -.
DR   PDBsum; 1UUP; -.
DR   AlphaFoldDB; P0DJY7; -.
DR   SMR; P0DJY7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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   Pfam; PF02876; Stap_Strp_tox_C; 1.
DR   Pfam; PF01123; Stap_Strp_toxin; 1.
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; Disulfide bond; Signal; Toxin; Virulence.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..250
FT                   /note="Exotoxin type A"
FT                   /id="PRO_0000035596"
FT   DISULFID        117..128
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   HELIX           49..56
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   HELIX           95..101
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:1L0X"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          126..130
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          140..153
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          156..170
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   HELIX           171..186
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          197..205
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:1UUP"
FT   STRAND          211..216
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   HELIX           223..226
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   HELIX           227..230
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:1L0Y"
FT   STRAND          240..248
FT                   /evidence="ECO:0007829|PDB:1L0Y"
SQ   SEQUENCE   250 AA;  29169 MW;  6D7F3EC8B2FDDED4 CRC64;
     MENNKEVLKK MVFFVLMKFL GLTILPKGIC STRPKPSQLQ RSNLVKTFKI YIFFMRVTLV
     THENVKSVDQ LLSHDLIYNV SGPNYDKLKT ELKNQEMATL FKDKNVDIYG VEYYHLCYLC
     ENAERSACLY GGVTNHEGNH LEIPKKIVVK VSIDGIQSLS FDIEQIKNGN CSRISYTVRK
     YLTDNKQLYT NGPSKYETGY IKFIPKNKES FWFDFFPEPE FTQSKYLMIY KDNETLDSNT
     SQIEVYLTTK