ENTC3_STAAU
ID ENTC3_STAAU Reviewed; 266 AA.
AC P0A0L5; P23313;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Enterotoxin type C-3;
DE AltName: Full=SEC3;
DE Flags: Precursor;
GN Name=entC3;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2325627; DOI=10.1007/bf00260504;
RA Hovde C.J., Hackett S.P., Bohach G.A.;
RT "Nucleotide sequence of the staphylococcal enterotoxin C3 gene: sequence
RT comparison of all three type C staphylococcal enterotoxins.";
RL Mol. Gen. Genet. 220:329-333(1990).
RN [2]
RP FUNCTION, AND INTERACTION WITH HOST MHC CLASS II HLA-DRA; HLA-DRB1 AND
RP T-CELL RECEPTOR/TCR BETA VARIABLE CHAIN.
RX PubMed=10229190; DOI=10.1016/s1074-7613(00)80047-3;
RA Andersen P.S., Lavoie P.M., Sekaly R.P., Churchill H., Kranz D.M.,
RA Schlievert P.M., Karjalainen K., Mariuzza R.A.;
RT "Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-
RT MHC class II complexes.";
RL Immunity 10:473-483(1999).
RN [3]
RP FUNCTION.
RX PubMed=28849041; DOI=10.3892/mmr.2017.7199;
RA Xie Y., Wang M., Dong Z., Song H., Li L., Yang M., Li P., Tian J.,
RA Zhang K., Xia X., Zhang T., Tang A.;
RT "In vitro effects of Staphylococcus aureus enterotoxin C3 on T cell
RT activation, proliferation and cytokine production.";
RL Mol. Med. Report. 16:4744-4750(2017).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF COMPLEX WITH HOST TCR, AND
RP DISULFIDE BOND.
RX PubMed=8906797; DOI=10.1038/384188a0;
RA Fields B.A., Malchiodi E.L., Li H., Ysern X., Stauffacher C.V.,
RA Schlievert P.M., Karjalainen K., Mariuzza R.A.;
RT "Crystal structure of a T-cell receptor beta-chain complexed with a
RT superantigen.";
RL Nature 384:188-192(1996).
RN [5] {ECO:0007744|PDB:1JWM, ECO:0007744|PDB:1JWS, ECO:0007744|PDB:1JWU}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 28-266, INTERACTION WITH HOST MHC
RP CLASS II SUBUNITS HLA-DRA AND HLA-DRB1, AND DISULFIDE BOND.
RX PubMed=12962633; DOI=10.1016/s0969-2126(03)00187-4;
RA Sundberg E.J., Andersen P.S., Schlievert P.M., Karjalainen K.,
RA Mariuzza R.A.;
RT "Structural, energetic, and functional analysis of a protein-protein
RT interface at distinct stages of affinity maturation.";
RL Structure 11:1151-1161(2003).
RN [6] {ECO:0007744|PDB:3BVM, ECO:0007744|PDB:3BVZ, ECO:0007744|PDB:3BYT, ECO:0007744|PDB:3BYY, ECO:0007744|PDB:3BZD}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-266 IN COMPLEX WITH ZINC.
RA Cho S., Swaminathan C.P., Kerzic M.C., Guan R., Yang J., Kieke M.C.,
RA Andersen P.S., Krantz D.M., Mariuzza R.A., Eric S.J.;
RT "Manipulating the coupled folding and binding process drives affinity
RT maturation in a protein-protein complex.";
RL Submitted (JAN-2008) to the PDB data bank.
RN [7] {ECO:0007744|PDB:3BVG}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-266 IN COMPLEX WITH ZINC, AND
RP INTERACTION WITH HOST T-CELL RECEPTOR/TCR BETA VARIABLE/TRBV8-2.
RX PubMed=20836565; DOI=10.1021/bi1008968;
RA Cho S., Swaminathan C.P., Bonsor D.A., Kerzic M.C., Guan R., Yang J.,
RA Kieke M.C., Andersen P.S., Kranz D.M., Mariuzza R.A., Sundberg E.J.;
RT "Assessing energetic contributions to binding from a disordered region in a
RT protein-protein interaction.";
RL Biochemistry 49:9256-9268(2010).
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:10229190, PubMed:28849041). Causes also the intoxication
CC staphylococcal food poisoning syndrome (By similarity).
CC {ECO:0000250|UniProtKB:P34071, ECO:0000269|PubMed:10229190,
CC ECO:0000269|PubMed:28849041}.
CC -!- SUBUNIT: Interacts with MHC class II molecules composed of alpha/HLA-
CC DRA and beta/HLA-DRB1 chains (PubMed:10229190). Interacts with host T-
CC cell receptor/TCR beta variable chain TRBV8-2 (PubMed:10229190,
CC PubMed:20836565). {ECO:0000269|PubMed:10229190,
CC ECO:0000269|PubMed:20836565}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC {ECO:0000305}.
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DR EMBL; X51661; CAA35972.1; -; Genomic_DNA.
DR PIR; S11885; S11885.
DR RefSeq; WP_000278088.1; NZ_WJTW01000001.1.
DR PDB; 1JCK; X-ray; 3.50 A; B/D=28-266.
DR PDB; 1JWM; X-ray; 2.70 A; D=28-266.
DR PDB; 1JWS; X-ray; 2.60 A; D=28-266.
DR PDB; 1JWU; X-ray; 2.30 A; D=28-266.
DR PDB; 1KLG; X-ray; 2.40 A; D=28-266.
DR PDB; 1KLU; X-ray; 1.93 A; D=28-266.
DR PDB; 1SJE; X-ray; 2.45 A; D=28-266.
DR PDB; 1SJH; X-ray; 2.25 A; D=28-266.
DR PDB; 1T5X; X-ray; 2.50 A; D=28-266.
DR PDB; 2AQ1; X-ray; 2.10 A; B/D/F/H=28-266.
DR PDB; 2AQ2; X-ray; 1.80 A; B=28-266.
DR PDB; 2AQ3; X-ray; 2.30 A; B/D/F/H=28-266.
DR PDB; 2IPK; X-ray; 2.30 A; D=28-266.
DR PDB; 3BVG; X-ray; 2.00 A; A=28-266.
DR PDB; 3BVM; X-ray; 2.00 A; A=28-266.
DR PDB; 3BVZ; X-ray; 2.30 A; A=28-266.
DR PDB; 3BYT; X-ray; 2.30 A; B/D/F/H=28-266.
DR PDB; 3BYY; X-ray; 2.20 A; B=28-266.
DR PDB; 3BZD; X-ray; 2.30 A; B=28-266.
DR PDBsum; 1JCK; -.
DR PDBsum; 1JWM; -.
DR PDBsum; 1JWS; -.
DR PDBsum; 1JWU; -.
DR PDBsum; 1KLG; -.
DR PDBsum; 1KLU; -.
DR PDBsum; 1SJE; -.
DR PDBsum; 1SJH; -.
DR PDBsum; 1T5X; -.
DR PDBsum; 2AQ1; -.
DR PDBsum; 2AQ2; -.
DR PDBsum; 2AQ3; -.
DR PDBsum; 2IPK; -.
DR PDBsum; 3BVG; -.
DR PDBsum; 3BVM; -.
DR PDBsum; 3BVZ; -.
DR PDBsum; 3BYT; -.
DR PDBsum; 3BYY; -.
DR PDBsum; 3BZD; -.
DR AlphaFoldDB; P0A0L5; -.
DR SMR; P0A0L5; -.
DR Allergome; 2141; Sta a SEC.
DR OMA; KFTGLME; -.
DR EvolutionaryTrace; P0A0L5; -.
DR PRO; PR:P0A0L5; -.
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 CHAIN 28..266
FT /note="Enterotoxin type C-3"
FT /id="PRO_0000035611"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20836565, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:3BVG, ECO:0007744|PDB:3BVM,
FT ECO:0007744|PDB:3BVZ"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20836565, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:3BVG, ECO:0007744|PDB:3BVM,
FT ECO:0007744|PDB:3BVZ"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20836565, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:3BVG, ECO:0007744|PDB:3BVM,
FT ECO:0007744|PDB:3BVZ"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20836565, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:3BVG, ECO:0007744|PDB:3BVM,
FT ECO:0007744|PDB:3BVZ"
FT DISULFID 120..137
FT /evidence="ECO:0000269|PubMed:12962633,
FT ECO:0000269|PubMed:20836565, ECO:0000269|PubMed:8906797,
FT ECO:0000269|Ref.6, ECO:0007744|PDB:1JCK,
FT ECO:0007744|PDB:1JWM, ECO:0007744|PDB:1JWS,
FT ECO:0007744|PDB:1JWU, ECO:0007744|PDB:3BVG,
FT ECO:0007744|PDB:3BVM, ECO:0007744|PDB:3BVZ,
FT ECO:0007744|PDB:3BYT, ECO:0007744|PDB:3BYY,
FT ECO:0007744|PDB:3BZD"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2AQ2"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2AQ2"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2AQ2"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3BZD"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 83..94
FT /evidence="ECO:0007829|PDB:2AQ2"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2AQ2"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3BZD"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1KLU"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 167..182
FT /evidence="ECO:0007829|PDB:2AQ2"
FT HELIX 183..198
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1JWU"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:2AQ2"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3BZD"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2AQ2"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:2AQ2"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:2AQ2"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2AQ2"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:2AQ2"
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
