ENTC2_STAAU
ID ENTC2_STAAU Reviewed; 266 AA.
AC P34071;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Enterotoxin type C-2;
DE AltName: Full=SEC2;
DE Flags: Precursor;
GN Name=entC2;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-66.
RX PubMed=2543637; DOI=10.1128/iai.57.7.2249-2252.1989;
RA Bohach G.A., Schlievert P.M.;
RT "Conservation of the biologically active portions of staphylococcal
RT enterotoxins C1 and C2.";
RL Infect. Immun. 57:2249-2252(1989).
RN [2]
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 [3]
RP FUNCTION, AND MUTAGENESIS OF HIS-74; HIS-145 AND HIS-149.
RC STRAIN=0165;
RX PubMed=19246739; DOI=10.1099/mic.0.025254-0;
RA Wang X., Zhang H., Xu M., Cai Y., Liu C., Su Z., Zhang C.;
RT "Biological characterization of the zinc site coordinating histidine
RT residues of staphylococcal enterotoxin C2.";
RL Microbiology 155:680-686(2009).
RN [4] {ECO:0007744|PDB:1STE}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC.
RX PubMed=7582894; DOI=10.1016/s0969-2126(01)00212-x;
RA Papageorgiou A.C., Acharya K.R., Shapiro R., Passalacqua E.F., Brehm R.D.,
RA Tranter H.S.;
RT "Crystal structure of the superantigen enterotoxin C2 from Staphylococcus
RT aureus reveals a zinc-binding site.";
RL Structure 3:769-779(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=7552730; DOI=10.1038/nsb0895-680;
RA Swaminathan S., Furey W.F. Jr., Pletcher J., Sax M.;
RT "Residues defining V beta specificity in staphylococcal enterotoxins.";
RL Nat. Struct. Biol. 2:680-686(1995).
RN [6]
RP COMPARISON OF STRUCTURE OF SEA AND SEC2.
RX PubMed=9191070; DOI=10.1006/jmbi.1997.1023;
RA Schad E.M., Papageorgiou A.C., Svensson L.A., Acharya K.R.;
RT "A structural and functional comparison of staphylococcal enterotoxins A
RT and C2 reveals remarkable similarity and dissimilarity.";
RL J. Mol. Biol. 269:270-280(1997).
RN [7] {ECO:0007744|PDB:1CQV, ECO:0007744|PDB:1I4P, ECO:0007744|PDB:1I4Q, ECO:0007744|PDB:1I4R, ECO:0007744|PDB:1I4X}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-266 IN COMPLEX WITH ZINC, AND
RP DISULFIDE BONDS.
RX PubMed=11526318; DOI=10.1107/s0907444901011118;
RA Kumaran D., Eswaramoorthy S., Furey W., Sax M., Swaminathan S.;
RT "Structure of staphylococcal enterotoxin C2 at various pH levels.";
RL Acta Crystallogr. D 57:1270-1275(2001).
RN [8] {ECO:0007744|PDB:1UNS}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-266 IN COMPLEX WITH ZINC,
RP DISULFIDE BONDS, AND FUNCTION.
RX PubMed=14559915; DOI=10.1074/jbc.m307333200;
RA Papageorgiou A.C., Baker M.D., McLeod J.D., Goda S.K., Manzotti C.N.,
RA Sansom D.M., Tranter H.S., Acharya K.R.;
RT "Identification of a secondary zinc-binding site in staphylococcal
RT enterotoxin C2. Implications for superantigen recognition.";
RL J. Biol. Chem. 279:1297-1303(2004).
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:19246739, PubMed:14559915). Causes also the
CC intoxication staphylococcal food poisoning syndrome (PubMed:19246739).
CC {ECO:0000269|PubMed:14559915, ECO:0000269|PubMed:19246739,
CC ECO:0000269|PubMed:2210803}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Possesses two zinc-binding sites. The zinc ion is necessary for
CC the toxin interaction with MHC class II. {ECO:0000269|PubMed:14559915};
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 PIR; A60114; A60114.
DR RefSeq; WP_001043552.1; NZ_WKII01000007.1.
DR PDB; 1CQV; X-ray; 2.06 A; A=28-266.
DR PDB; 1I4P; X-ray; 2.00 A; A=28-266.
DR PDB; 1I4Q; X-ray; 2.20 A; A=28-266.
DR PDB; 1I4R; X-ray; 2.10 A; A=28-266.
DR PDB; 1I4X; X-ray; 2.40 A; A=28-266.
DR PDB; 1SE2; X-ray; 2.70 A; A=28-266.
DR PDB; 1STE; X-ray; 2.00 A; A=28-266.
DR PDB; 1UNS; X-ray; 2.00 A; A=28-266.
DR PDBsum; 1CQV; -.
DR PDBsum; 1I4P; -.
DR PDBsum; 1I4Q; -.
DR PDBsum; 1I4R; -.
DR PDBsum; 1I4X; -.
DR PDBsum; 1SE2; -.
DR PDBsum; 1STE; -.
DR PDBsum; 1UNS; -.
DR AlphaFoldDB; P34071; -.
DR SMR; P34071; -.
DR Allergome; 2141; Sta a SEC.
DR EvolutionaryTrace; P34071; -.
DR PRO; PR:P34071; -.
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; Direct protein sequencing; Disulfide bond; Enterotoxin;
KW Metal-binding; Secreted; Signal; Superantigen; Toxin; Virulence; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:2543637"
FT CHAIN 28..266
FT /note="Enterotoxin type C-2"
FT /id="PRO_0000035608"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|PubMed:11526318,
FT ECO:0000269|PubMed:14559915, ECO:0000269|PubMed:7582894,
FT ECO:0007744|PDB:1CQV, ECO:0007744|PDB:1I4P,
FT ECO:0007744|PDB:1I4Q, ECO:0007744|PDB:1I4R,
FT ECO:0007744|PDB:1STE, ECO:0007744|PDB:1UNS"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14559915,
FT ECO:0007744|PDB:1UNS"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14559915,
FT ECO:0007744|PDB:1UNS"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14559915,
FT ECO:0007744|PDB:1UNS"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11526318,
FT ECO:0000269|PubMed:14559915, ECO:0000269|PubMed:7582894,
FT ECO:0007744|PDB:1CQV, ECO:0007744|PDB:1I4P,
FT ECO:0007744|PDB:1I4Q, ECO:0007744|PDB:1I4R,
FT ECO:0007744|PDB:1I4X, ECO:0007744|PDB:1STE,
FT ECO:0007744|PDB:1UNS"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11526318,
FT ECO:0000269|PubMed:14559915, ECO:0000269|PubMed:7582894,
FT ECO:0007744|PDB:1CQV, ECO:0007744|PDB:1I4P,
FT ECO:0007744|PDB:1I4Q, ECO:0007744|PDB:1I4R,
FT ECO:0007744|PDB:1I4X, ECO:0007744|PDB:1STE,
FT ECO:0007744|PDB:1UNS"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:14559915,
FT ECO:0007744|PDB:1UNS"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11526318,
FT ECO:0000269|PubMed:14559915, ECO:0000269|PubMed:7582894,
FT ECO:0007744|PDB:1CQV, ECO:0007744|PDB:1I4P,
FT ECO:0007744|PDB:1I4Q, ECO:0007744|PDB:1I4R,
FT ECO:0007744|PDB:1I4X, ECO:0007744|PDB:1STE,
FT ECO:0007744|PDB:1UNS"
FT DISULFID 120..137
FT /evidence="ECO:0000269|PubMed:14559915,
FT ECO:0000269|PubMed:7582894, ECO:0007744|PDB:1CQV,
FT ECO:0007744|PDB:1I4P, ECO:0007744|PDB:1I4Q,
FT ECO:0007744|PDB:1I4R, ECO:0007744|PDB:1I4X,
FT ECO:0007744|PDB:1SE2, ECO:0007744|PDB:1STE,
FT ECO:0007744|PDB:1UNS"
FT MUTAGEN 74
FT /note="H->A: About 30% loss of T-cell stimulation."
FT /evidence="ECO:0000269|PubMed:19246739"
FT MUTAGEN 145
FT /note="H->A: Complete loss of emetic activity."
FT /evidence="ECO:0000269|PubMed:19246739"
FT MUTAGEN 149
FT /note="H->A: Complete loss of emetic activity."
FT /evidence="ECO:0000269|PubMed:19246739"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1I4P"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1I4P"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1I4P"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1I4P"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:1I4P"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1UNS"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1I4P"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1STE"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 168..182
FT /evidence="ECO:0007829|PDB:1I4P"
FT HELIX 183..198
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1I4P"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:1I4P"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1I4P"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:1I4P"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1I4P"
SQ SEQUENCE 266 AA; 30604 MW; 8407FB18536FAC08 CRC64;
MNKSRFISCV ILIFALILVL FTPNVLAESQ PDPTPDELHK SSEFTGTMGN MKYLYDDHYV
SATKVMSVDK FLAHDLIYNI SDKKLKNYDK VKTELLNEDL AKKYKDEVVD VYGSNYYVNC
YFSSKDNVGK VTGGKTCMYG GITKHEGNHF DNGNLQNVLI RVYENKRNTI SFEVQTDKKS
VTAQELDIKA RNFLINKKNL YEFNSSPYET GYIKFIENNG NTFWYDMMPA PGDKFDQSKY
LMMYNDNKTV DSKSVKIEVH LTTKNG
