ENTC3_STAAM
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 03-AUG-2022, entry version 94.
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; Firmicutes; 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}.
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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 PaxDb; P0A0L3; -.
DR EnsemblBacteria; BAB58171; BAB58171; SAV2009.
DR KEGG; sav:SAV2009; -.
DR HOGENOM; CLU_093855_0_1_9; -.
DR OMA; KFTGLME; -.
DR PhylomeDB; P0A0L3; -.
DR BioCyc; SAUR158878:SAV_RS10980-MON; -.
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 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; 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
