ID ENTC3_STAAM Reviewed; 266 AA. AC P0A0L3; P23313; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Enterotoxin type C-3; DE AltName: Full=SEC3; DE Flags: Precursor; GN Name=entC3; OrderedLocusNames=SAV2009; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu50 / ATCC 700699; 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}. 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; BA000017; BAB58171.1; -; Genomic_DNA. DR RefSeq; WP_000278088.1; NC_002758.2. DR PDB; 1PYW; X-ray; 2.10 A; D=28-266. DR PDBsum; 1PYW; -. DR AlphaFoldDB; P0A0L3; -. DR SMR; P0A0L3; -. DR Allergome; 2141; Sta a SEC. DR KEGG; sav:SAV2009; -. DR HOGENOM; CLU_093855_0_1_9; -. DR PhylomeDB; P0A0L3; -. DR PRO; PR:P0A0L3; -. DR Proteomes; UP000002481; 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 Gene3D; 2.40.50.110; -; 1. DR Gene3D; 3.10.20.120; -; 1. 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; Bacterial enterotoxins; 1. DR SUPFAM; SSF54334; Superantigen toxins, C-terminal domain; 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; Enterotoxin; Metal-binding; Secreted; Signal; KW Superantigen; Toxin; Virulence; Zinc. FT SIGNAL 1..27 FT /evidence="ECO:0000250" FT CHAIN 28..266 FT /note="Enterotoxin type C-3" FT /id="PRO_0000035609" FT DISULFID 120..137 FT /evidence="ECO:0000250" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:1PYW" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:1PYW" FT HELIX 49..55 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 75..79 FT /evidence="ECO:0007829|PDB:1PYW" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 89..94 FT /evidence="ECO:0007829|PDB:1PYW" FT HELIX 98..105 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 109..113 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 135..139 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:1PYW" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 156..164 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 167..182 FT /evidence="ECO:0007829|PDB:1PYW" FT HELIX 183..198 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 209..216 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:1PYW" FT HELIX 237..241 FT /evidence="ECO:0007829|PDB:1PYW" FT HELIX 242..246 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 249..251 FT /evidence="ECO:0007829|PDB:1PYW" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:1PYW" FT STRAND 256..262 FT /evidence="ECO:0007829|PDB:1PYW" 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 //