ID   SPEC_STRP8              Reviewed;         235 AA.
AC   Q8NKX2; P13380;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Exotoxin type C;
DE   AltName: Full=SPE C;
DE   Flags: Precursor;
GN   Name=speC; OrderedLocusNames=spyM18_0778;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-52.
RC   STRAIN=MGAS1585 / Serotype M18;
RX   PubMed=3045005; DOI=10.1128/iai.56.9.2518-2520.1988;
RA   Goshorn S.C., Schlievert P.M.;
RT   "Nucleotide sequence of streptococcal pyrogenic exotoxin type C.";
RL   Infect. Immun. 56:2518-2520(1988).
RN   [2]
RP   SEQUENCE REVISION TO 21-26.
RC   STRAIN=MGAS1585 / Serotype M18;
RX   PubMed=1500157; DOI=10.1128/iai.60.9.3513-3517.1992;
RA   Kapur V., Nelson K., Schlievert P.M., Selander R.K., Musser J.M.;
RT   "Molecular population genetic evidence of horizontal spread of two alleles
RT   of the pyrogenic exotoxin C gene (speC) among pathogenic clones of
RT   Streptococcus pyogenes.";
RL   Infect. Immun. 60:3513-3517(1992).
RN   [3]
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   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-235, AND MISCELLANEOUS.
RX   PubMed=9253413; DOI=10.1038/nsb0897-635;
RA   Roussel A., Anderson B.F., Baker H.M., Fraser J.D., Baker E.N.;
RT   "Crystal structure of the streptococcal superantigen SPE-C: dimerization
RT   and zinc binding suggest a novel mode of interaction with MHC class II
RT   molecules.";
RL   Nat. Struct. Biol. 4:635-643(1997).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 28-235 IN COMPLEX WITH
RP   HLA-DRA/HLA-DRB5 HETERODIMER WITH MPB PEPTIDE, AND MISCELLANEOUS.
RX   PubMed=11163233; DOI=10.1016/s1074-7613(01)00092-9;
RA   Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P.,
RA   Schlievert P.M., Mariuzza R.A.;
RT   "Crystal structure of a superantigen bound to the high-affinity, zinc-
RT   dependent site on MHC class II.";
RL   Immunity 14:93-104(2001).
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: Superantigen that binds to major histocompatibility
CC       complex class II beta chain in a zinc-dependent manner, it may activate
CC       up to 20% of all T-cells. Superantigens bind simultaneously TCRs and
CC       MHC class II molecules resulting in a massive release of pyrogenic and
CC       inflammatory cytokines.
CC   -!- MISCELLANEOUS: This toxin seems to be coded by a bacteriophage.
CC   -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M35514; AAA27017.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M97156; AAB59091.1; -; Genomic_DNA.
DR   EMBL; M97157; AAB59092.1; -; Genomic_DNA.
DR   EMBL; AE009949; AAL97445.1; -; Genomic_DNA.
DR   PIR; A30509; A30509.
DR   PIR; A44799; A44799.
DR   RefSeq; WP_002985327.1; NC_003485.1.
DR   PDB; 1AN8; X-ray; 2.40 A; A=28-235.
DR   PDB; 1HQR; X-ray; 3.20 A; D=28-235.
DR   PDB; 1KTK; X-ray; 3.00 A; A/B/C/D=28-235.
DR   PDBsum; 1AN8; -.
DR   PDBsum; 1HQR; -.
DR   PDBsum; 1KTK; -.
DR   AlphaFoldDB; Q8NKX2; -.
DR   SMR; Q8NKX2; -.
DR   Allergome; 8279; Str py SPEC.
DR   KEGG; spm:spyM18_0778; -.
DR   HOGENOM; CLU_093855_1_0_9; -.
DR   EvolutionaryTrace; Q8NKX2; -.
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; Direct protein sequencing; Signal; Toxin; Virulence.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:3045005"
FT   CHAIN           28..235
FT                   /note="Exotoxin type C"
FT                   /id="PRO_0000035598"
FT   HELIX           33..44
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          49..59
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   HELIX           69..72
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   HELIX           84..87
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          95..100
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          131..135
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   HELIX           156..171
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          173..177
FT                   /evidence="ECO:0007829|PDB:1KTK"
FT   STRAND          182..189
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          194..200
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   HELIX           208..212
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   HELIX           213..217
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:1AN8"
FT   STRAND          226..234
FT                   /evidence="ECO:0007829|PDB:1AN8"
SQ   SEQUENCE   235 AA;  27372 MW;  53EBD041B958C65B CRC64;
     MKKINIIKIV FIITVILIST ISPIIKSDSK KDISNVKSDL LYAYTITPYD YKDCRVNFST
     THTLNIDTQK YRGKDYYISS EMSYEASQKF KRDDHVDVFG LFYILNSHTG EYIYGGITPA
     QNNKVNHKLL GNLFISGESQ QNLNNKIILE KDIVTFQEID FKIRKYLMDN YKIYDATSPY
     VSGRIEIGTK DGKHEQIDLF DSPNEGTRSD IFAKYKDNRI INMKNFSHFD IYLEK