ETXD_STAAU
ID ETXD_STAAU Reviewed; 258 AA.
AC P20723;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Enterotoxin type D;
DE AltName: Full=SED;
DE Flags: Precursor;
GN Name=entD;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2549000; DOI=10.1128/jb.171.9.4799-4806.1989;
RA Bayles K.W., Iandolo J.J.;
RT "Genetic and molecular analyses of the gene encoding staphylococcal
RT enterotoxin D.";
RL J. Bacteriol. 171:4799-4806(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN
RP COMPLEX WITH ZINC, SUBUNIT, AND INTERACTION WITH HOST HLA-DRA AND HLA-DRB1.
RC STRAIN=ATCC 23235 / NCTC 10656;
RX PubMed=9003758; DOI=10.1002/j.1460-2075.1996.tb01074.x;
RA Sundstroem M., Abrahmsen L., Antonsson P., Mehindate K., Mourad W.,
RA Dohlsten M.;
RT "The crystal structure of staphylococcal enterotoxin type D reveals Zn2+-
RT mediated homodimerization.";
RL EMBO J. 15:6832-6840(1996).
RN [3]
RP FUNCTION.
RX PubMed=8621894;
RA Domiati-Saad R., Attrep J.F., Brezinschek H.P., Cherrie A.H., Karp D.R.,
RA Lipsky P.E.;
RT "Staphylococcal enterotoxin D functions as a human B cell superantigen by
RT rescuing VH4-expressing B cells from apoptosis.";
RL J. Immunol. 156:3608-3620(1996).
RN [4]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-72; ASP-212; HIS-248 AND ASP-252, AND
RP INTERACTION WITH HOST HLA-DRB1.
RX PubMed=9551975;
RA Al-Daccak R., Mehindate K., Damdoumi F., Etongue-Mayer P., Nilsson H.,
RA Antonsson P., Sundstroem M., Dohlsten M., Sekaly R.P., Mourad W.;
RT "Staphylococcal enterotoxin D is a promiscuous superantigen offering
RT multiple modes of interactions with the MHC class II receptors.";
RL J. Immunol. 160:225-232(1998).
RN [5]
RP FUNCTION.
RX PubMed=17306397; DOI=10.1016/j.ijfoodmicro.2006.10.050;
RA Kerouanton A., Hennekinne J.A., Letertre C., Petit L., Chesneau O.,
RA Brisabois A., De Buyser M.L.;
RT "Characterization of Staphylococcus aureus strains associated with food
RT poisoning outbreaks in France.";
RL Int. J. Food Microbiol. 115:369-375(2007).
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:9551975). In addition, induces B-cell proliferation and
CC differentiation in the presence of T-cells (PubMed:8621894). Causes
CC also the intoxication staphylococcal food poisoning syndrome
CC (PubMed:17306397). {ECO:0000269|PubMed:17306397,
CC ECO:0000269|PubMed:8621894, ECO:0000269|PubMed:9551975}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=A zinc-binding site contributes directly to formation of the
CC homodimer. {ECO:0000269|PubMed:9003758};
CC -!- SUBUNIT: Homodimer; zinc-dependent (PubMed:9003758). Interacts with MHC
CC class II molecules composed of alpha/HLA-DRA and beta/HLA-DRB1 chains
CC (PubMed:9003758, PubMed:9551975). {ECO:0000269|PubMed:9003758,
CC ECO:0000269|PubMed:9551975}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC {ECO:0000305}.
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DR EMBL; M28521; AAB06195.1; -; Genomic_DNA.
DR PIR; A33953; A33953.
DR AlphaFoldDB; P20723; -.
DR SMR; P20723; -.
DR Allergome; 2142; Sta a SED.
DR PRO; PR:P20723; -.
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; IDA:UniProtKB.
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 Enterotoxin; Metal-binding; Secreted; Signal; Superantigen; Toxin;
KW Virulence; Zinc.
FT SIGNAL 1..25
FT CHAIN 26..258
FT /note="Enterotoxin type D"
FT /id="PRO_0000035612"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:9003758"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|PubMed:9003758"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:9003758"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:9003758"
FT VARIANT 114
FT /note="P -> A (in strain: ATCC 23235)"
FT MUTAGEN 72
FT /note="F->A: Complete loss of host cytokine gene
FT expression."
FT /evidence="ECO:0000269|PubMed:9551975"
FT MUTAGEN 212
FT /note="D->A: Complete loss of host cytokine gene
FT expression."
FT /evidence="ECO:0000269|PubMed:9551975"
FT MUTAGEN 248
FT /note="H->A: Complete loss of host cytokine gene
FT expression."
FT /evidence="ECO:0000269|PubMed:9551975"
FT MUTAGEN 252
FT /note="D->A: Complete loss of host cytokine gene
FT expression."
FT /evidence="ECO:0000269|PubMed:9551975"
SQ SEQUENCE 258 AA; 29746 MW; 4F7C6A28D42597FD CRC64;
MKKFNILIAL LFFTSLVISP LNVKANENID SVKEKELHKK SELSSTALNN MKHSYADKNP
IIGENKSTGD QFLENTLLYK KFFTDLINFE DLLINFNSKE MAQHFKSKNV DVYPIRYSIN
CYGGEIDRTA CTYGGVTPHE GNKLKERKKI PINLWINGVQ KEVSLDKVQT DKKNVTVQEL
DAQARRYLQK DLKLYNNDTL GGKIQRGKIE FDSSDGSKVS YDLFDVKGDF PEKQLRIYSD
NKTLSTEHLH IDIYLYEK
