ENTC3_STAAN
ID ENTC3_STAAN Reviewed; 266 AA.
AC P0A0L4; P23313;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Enterotoxin type C-3;
DE AltName: Full=SEC3;
DE Flags: Precursor;
GN Name=entC3; OrderedLocusNames=SA1817;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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 (By
CC similarity). Causes also the intoxication staphylococcal food poisoning
CC syndrome (By similarity). {ECO:0000250|UniProtKB:P0A0L5,
CC ECO:0000250|UniProtKB:P34071}.
CC -!- SUBUNIT: Interacts with MHC class II molecules composed of alpha/HLA-
CC DRA and beta/HLA-DRB1 chains. Interacts with host T-cell receptor/TCR
CC beta variable chain TRBV8-2. {ECO:0000250|UniProtKB:P0A0L5}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC {ECO:0000305}.
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DR EMBL; BA000018; BAB43097.1; -; Genomic_DNA.
DR RefSeq; WP_000278088.1; NC_002745.2.
DR AlphaFoldDB; P0A0L4; -.
DR SMR; P0A0L4; -.
DR Allergome; 2141; Sta a SEC.
DR EnsemblBacteria; BAB43097; BAB43097; BAB43097.
DR KEGG; sau:SA1817; -.
DR HOGENOM; CLU_093855_0_1_9; -.
DR OMA; KFTGLME; -.
DR PRO; PR:P0A0L4; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Disulfide bond; Enterotoxin; Metal-binding; Secreted; Signal; Superantigen;
KW Toxin; Virulence; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..266
FT /note="Enterotoxin type C-3"
FT /id="PRO_0000035610"
FT DISULFID 120..137
FT /evidence="ECO:0000250"
SQ SEQUENCE 266 AA; 30671 MW; 5ED8A32D11FFCA59 CRC64;
MYKRLFISRV ILIFALILVI STPNVLAESQ PDPMPDDLHK SSEFTGTMGN MKYLYDDHYV
SATKVKSVDK FLAHDLIYNI SDKKLKNYDK VKTELLNEDL AKKYKDEVVD VYGSNYYVNC
YFSSKDNVGK VTGGKTCMYG GITKHEGNHF DNGNLQNVLV RVYENKRNTI SFEVQTDKKS
VTAQELDIKA RNFLINKKNL YEFNSSPYET GYIKFIENNG NTFWYDMMPA PGDKFDQSKY
LMMYNDNKTV DSKSVKIEVH LTTKNG