ID   ENTC1_STAAU             Reviewed;         266 AA.
AC   P01553;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Enterotoxin type C-1;
DE   AltName: Full=SEC1;
DE   Flags: Precursor;
GN   Name=entC1;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2823067; DOI=10.1007/bf00329830;
RA   Bohach G.A., Schlievert P.M.;
RT   "Nucleotide sequence of the staphylococcal enterotoxin C1 gene and
RT   relatedness to other pyrogenic toxins.";
RL   Mol. Gen. Genet. 209:15-20(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-266.
RX   PubMed=6189824; DOI=10.1016/s0021-9258(18)32408-6;
RA   Schmidt J.J., Spero L.;
RT   "The complete amino acid sequence of staphylococcal enterotoxin C1.";
RL   J. Biol. Chem. 258:6300-6306(1983).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH HOST MHC II HLA-DRA AND HLA-DRB1.
RX   PubMed=2210803;
RA   Dohlsten M., Lando P.A., Hedlund G., Trowsdale J., Kalland T.;
RT   "Targeting of human cytotoxic T lymphocytes to MHC class II-expressing
RT   cells by staphylococcal enterotoxins.";
RL   Immunology 71:96-100(1990).
RN   [4]
RP   FUNCTION.
RX   PubMed=8039910; DOI=10.1128/iai.62.8.3396-3407.1994;
RA   Hoffmann M.L., Jablonski L.M., Crum K.K., Hackett S.P., Chi Y.I.,
RA   Stauffacher C.V., Stevens D.L., Bohach G.A.;
RT   "Predictions of T-cell receptor- and major histocompatibility complex-
RT   binding sites on staphylococcal enterotoxin C1.";
RL   Infect. Immun. 62:3396-3407(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=9498747;
RA   Lamphear J.G., Bohach G.A., Rich R.R.;
RT   "Structural dichotomy of staphylococcal enterotoxin C superantigens leading
RT   to MHC class II-independent activation of T lymphocytes.";
RL   J. Immunol. 160:2107-2114(1998).
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. In turn,
CC       this ternary complex activates a large number of T-lymphocytes
CC       initiating a systemic release of pro-inflammatory cytokines
CC       (PubMed:2210803, PubMed:8039910). Inhibits SEC1-mediated T-cell
CC       activation in the absence of MHC class II by competing with SEC1 for
CC       binding to the host TCR (PubMed:9498747). Causes also the intoxication
CC       staphylococcal food poisoning syndrome (By similarity).
CC       {ECO:0000250|UniProtKB:P34071, ECO:0000269|PubMed:2210803,
CC       ECO:0000269|PubMed:8039910, ECO:0000269|PubMed:9498747}.
CC   -!- SUBUNIT: Interacts with host MHC class II molecules composed of
CC       alpha/HLA-DRA and beta/HLA-DRB1 chains. {ECO:0000269|PubMed:2210803}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC       {ECO:0000305}.
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DR   EMBL; X05815; CAA29260.1; -; Genomic_DNA.
DR   PIR; S06356; ENSAC1.
DR   RefSeq; WP_001043549.1; NZ_UHBW01000001.1.
DR   AlphaFoldDB; P01553; -.
DR   SMR; P01553; -.
DR   Allergome; 2141; Sta a SEC.
DR   ABCD; P01553; 11 sequenced antibodies.
DR   PRO; PR:P01553; -.
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; PS00277; STAPH_STREP_TOXIN_1; 1.
DR   PROSITE; PS00278; STAPH_STREP_TOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Enterotoxin; Secreted; Signal;
KW   Superantigen; Toxin; Virulence.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:6189824"
FT   CHAIN           28..266
FT                   /note="Enterotoxin type C-1"
FT                   /evidence="ECO:0000269|PubMed:6189824"
FT                   /id="PRO_0000035607"
FT   DISULFID        120..137
FT                   /evidence="ECO:0000269|PubMed:6189824"
FT   CONFLICT        177
FT                   /note="D -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   266 AA;  30546 MW;  3A7AB59A8986853B CRC64;
     MNKSRFISCV ILIFALILVL FTPNVLAESQ PDPTPDELHK ASKFTGLMEN MKVLYDDHYV
     SATKVKSVDK FLAHDLIYNI SDKKLKNYDK VKTELLNEGL AKKYKDEVVD VYGSNYYVNC
     YFSSKDNVGK VTGGKTCMYG GITKHEGNHF DNGNLQNVLI RVYENKRNTI SFEVQTDKKS
     VTAQELDIKA RNFLINKKNL YEFNSSPYET GYIKFIENNG NTFWYDMMPA PGDKFDQSKY
     LMMYNDNKTV DSKSVKIEVH LTTKNG