ID   SPEA_STRP8              Reviewed;         251 AA.
AC   P62561; P08095;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
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; OrderedLocusNames=spyM18_0393;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 31-251 IN COMPLEX WITH MOUSE TCR
RP   BETA, AND DISULFIDE BOND.
RX   PubMed=12015151; DOI=10.1016/s0969-2126(02)00759-1;
RA   Sundberg E.J., Li H., Llera A.S., McCormick J.K., Tormo J.,
RA   Schlievert P.M., Karjalainen K., Mariuzza R.A.;
RT   "Structures of two streptococcal superantigens bound to TCR beta chains
RT   reveal diversity in the architecture of T cell signaling complexes.";
RL   Structure 10:687-699(2002).
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       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Binds to major histocompatibility complex class II beta
CC       chain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC       {ECO:0000305}.
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DR   EMBL; AE009949; AAL97141.1; -; Genomic_DNA.
DR   RefSeq; WP_009880239.1; NC_003485.1.
DR   PDB; 1L0Y; X-ray; 2.50 A; B/D=31-251.
DR   PDBsum; 1L0Y; -.
DR   AlphaFoldDB; P62561; -.
DR   SMR; P62561; -.
DR   Allergome; 8278; Str py SPEA.
DR   PRIDE; P62561; -.
DR   KEGG; spm:spyM18_0393; -.
DR   HOGENOM; CLU_093855_0_1_9; -.
DR   OMA; NSHSFWY; -.
DR   EvolutionaryTrace; P62561; -.
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   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; Disulfide bond; Signal; Toxin; Virulence.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..251
FT                   /note="Exotoxin type A"
FT                   /id="PRO_0000035597"
FT   DISULFID        117..128
FT                   /evidence="ECO:0000269|PubMed:12015151"
SQ   SEQUENCE   251 AA;  29246 MW;  54001FE4CCCBFCC3 CRC64;
     MENNKKVLKK MVFFVLVTFL GLTISQEVFA QQDPDPSQLH RSSLVKNLQN IYFLYEGDPV
     THENVKSVDQ LLSHDLIYNV SGPNYDKLKT ELKNQEMATL FKDKNVDIYG VEYYHLCYLC
     ENAERSACIY GGVTNHEGNH LEIPKKIVVK VSIDGIQSLS FDIETNKKMV TAQELDYKVR
     KYLTDNKQLY TNGPSKYETG YIKFIPKNKE SFWFDFFPEP EFTQSKYLMI YKDNETLDSN
     TSQIEVYLTT K