ETXB_STAAU
ID ETXB_STAAU Reviewed; 266 AA.
AC P01552;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Enterotoxin type B;
DE AltName: Full=SEB;
DE Flags: Precursor;
GN Name=entB;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3957869; DOI=10.1128/jb.166.1.29-33.1986;
RA Jones C.L., Khan S.A.;
RT "Nucleotide sequence of the enterotoxin B gene from Staphylococcus
RT aureus.";
RL J. Bacteriol. 166:29-33(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-91.
RX PubMed=3898073; DOI=10.1073/pnas.82.17.5850;
RA Ranelli D.M., Jones C.L., Johns M.B., Mussey G.J., Khan S.A.;
RT "Molecular cloning of staphylococcal enterotoxin B gene in Escherichia coli
RT and Staphylococcus aureus.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5850-5854(1985).
RN [3]
RP PROTEIN SEQUENCE OF 28-266 (S-6).
RX PubMed=5470821; DOI=10.1016/s0021-9258(18)62957-6;
RA Huang I.-Y., Bergdoll M.S.;
RT "The primary structure of staphylococcal enterotoxin B. 3. The cyanogen
RT bromide peptides of reduced and aminoethylated enterotoxin B, and the
RT complete amino acid sequence.";
RL J. Biol. Chem. 245:3518-3525(1970).
RN [4]
RP FUNCTION.
RX PubMed=2303780; DOI=10.1084/jem.171.2.455;
RA Marrack P., Blackman M., Kushnir E., Kappler J.;
RT "The toxicity of staphylococcal enterotoxin B in mice is mediated by T
RT cells.";
RL J. Exp. Med. 171:455-464(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1436058; DOI=10.1038/359801a0;
RA Swaminathan S., Furey W.F. Jr., Pletcher J., Sax M.;
RT "Crystal structure of staphylococcal enterotoxin B, a superantigen.";
RL Nature 359:801-806(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH HOST MHC II HLA-DRA
RP AND HLA-DRB1.
RX PubMed=8152483; DOI=10.1038/368711a0;
RA Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., Chi Y.I.,
RA Stauffacher C., Strominger J.L., Wiley D.C.;
RT "Three-dimensional structure of a human class II histocompatibility
RT molecule complexed with superantigen.";
RL Nature 368:711-718(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH HOST TCR.
RX PubMed=9881971; DOI=10.1016/s1074-7613(00)80646-9;
RA Li H., Llera A., Tsuchiya D., Leder L., Ysern X., Schlievert P.M.,
RA Karjalainen K., Mariuzza R.A.;
RT "Three-dimensional structure of the complex between a T cell receptor beta
RT chain and the superantigen staphylococcal enterotoxin B.";
RL Immunity 9:807-816(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=9514739; DOI=10.1006/jmbi.1997.1577;
RA Papageorgiou A.C., Tranter H.S., Acharya K.R.;
RT "Crystal structure of microbial superantigen staphylococcal enterotoxin B
RT at 1.5-A resolution: implications for superantigen recognition by MHC class
RT II molecules and T-cell receptors.";
RL J. Mol. Biol. 277:61-79(1998).
RN [9] {ECO:0007744|PDB:3R8B}
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=21689661; DOI=10.1016/j.jmb.2011.06.009;
RA Bonsor D.A., Postel S., Pierce B.G., Wang N., Zhu P., Buonpane R.A.,
RA Weng Z., Kranz D.M., Sundberg E.J.;
RT "Molecular basis of a million-fold affinity maturation process in a
RT protein-protein interaction.";
RL J. Mol. Biol. 411:321-328(2011).
RN [10] {ECO:0007744|PDB:4C56}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 29-266, DISULFIDE BOND,
RP INTERACTION WITH HOST TRBV19 AND MHC II HLA-DRB1, AND FUNCTION.
RX PubMed=25015819; DOI=10.4049/jimmunol.1401268;
RA Rodstrom K.E., Elbing K., Lindkvist-Petersson K.;
RT "Structure of the superantigen staphylococcal enterotoxin B in complex with
RT TCR and peptide-MHC demonstrates absence of TCR-peptide contacts.";
RL J. Immunol. 193:1998-2004(2014).
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:2303780, PubMed:25015819). Causes also the intoxication
CC staphylococcal food poisoning syndrome (By similarity).
CC {ECO:0000250|UniProtKB:P34071, ECO:0000269|PubMed:2303780,
CC ECO:0000269|PubMed:25015819}.
CC -!- SUBUNIT: Interacts with MHC class II molecules composed of alpha/HLA-
CC DRA and beta/HLA-DRB1 chains (PubMed:8152483, PubMed:25015819).
CC Interacts with T-cell receptor beta variable 19/TRBV19 (PubMed:9881971,
CC PubMed:25015819). {ECO:0000269|PubMed:25015819,
CC ECO:0000269|PubMed:8152483, ECO:0000269|PubMed:9881971}.
CC -!- INTERACTION:
CC P01552; P10747-1: CD28; Xeno; NbExp=5; IntAct=EBI-1027464, EBI-15945088;
CC P01552; P42081-3: CD86; Xeno; NbExp=5; IntAct=EBI-1027464, EBI-15945259;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Lacks the zinc-binding site found in other members of
CC this family, such as staphylococcal enterotoxin A, C2 and D, thus it
CC possesses only one MHC class II binding site.
CC {ECO:0000305|PubMed:9514739}.
CC -!- SIMILARITY: Belongs to the staphylococcal/streptococcal toxin family.
CC {ECO:0000305}.
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DR EMBL; M11118; AAA88550.1; -; Genomic_DNA.
DR PIR; S27360; ENSAB6.
DR RefSeq; WP_000278085.1; NZ_WTUM01000027.1.
DR PDB; 1D5M; X-ray; 2.00 A; C=28-266.
DR PDB; 1D5X; X-ray; 2.45 A; C=28-266.
DR PDB; 1D5Z; X-ray; 2.00 A; C=28-266.
DR PDB; 1D6E; X-ray; 2.45 A; C=28-266.
DR PDB; 1GOZ; X-ray; 2.00 A; A/B=28-266.
DR PDB; 1SBB; X-ray; 2.40 A; B/D=28-266.
DR PDB; 1SE3; X-ray; 2.30 A; A=28-266.
DR PDB; 1SE4; X-ray; 1.90 A; A=28-266.
DR PDB; 1SEB; X-ray; 2.70 A; D/H=29-262.
DR PDB; 2SEB; X-ray; 2.50 A; D=28-266.
DR PDB; 3GP7; X-ray; 1.90 A; A/B=28-266.
DR PDB; 3R8B; X-ray; 2.95 A; A/C/E/G/I/K/M/O=28-266.
DR PDB; 3SEB; X-ray; 1.48 A; A=28-265.
DR PDB; 3W2D; X-ray; 3.10 A; A=28-266.
DR PDB; 4C56; X-ray; 2.90 A; C/I=29-266.
DR PDB; 4RGM; X-ray; 2.69 A; A/S=28-266.
DR PDB; 4RGN; X-ray; 2.70 A; A/S=28-266.
DR PDB; 4RGO; X-ray; 1.80 A; S=28-266.
DR PDBsum; 1D5M; -.
DR PDBsum; 1D5X; -.
DR PDBsum; 1D5Z; -.
DR PDBsum; 1D6E; -.
DR PDBsum; 1GOZ; -.
DR PDBsum; 1SBB; -.
DR PDBsum; 1SE3; -.
DR PDBsum; 1SE4; -.
DR PDBsum; 1SEB; -.
DR PDBsum; 2SEB; -.
DR PDBsum; 3GP7; -.
DR PDBsum; 3R8B; -.
DR PDBsum; 3SEB; -.
DR PDBsum; 3W2D; -.
DR PDBsum; 4C56; -.
DR PDBsum; 4RGM; -.
DR PDBsum; 4RGN; -.
DR PDBsum; 4RGO; -.
DR AlphaFoldDB; P01552; -.
DR SMR; P01552; -.
DR DIP; DIP-35541N; -.
DR IntAct; P01552; 3.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR Allergome; 2140; Sta a SEB.
DR UniLectin; P01552; -.
DR PRIDE; P01552; -.
DR ABCD; P01552; 17 sequenced antibodies.
DR EvolutionaryTrace; P01552; -.
DR PRO; PR:P01552; -.
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.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:5470821"
FT CHAIN 28..266
FT /note="Enterotoxin type B"
FT /id="PRO_0000035606"
FT DISULFID 120..140
FT /evidence="ECO:0000269|PubMed:21689661,
FT ECO:0000269|PubMed:25015819, ECO:0007744|PDB:3R8B,
FT ECO:0007744|PDB:4C56"
FT CONFLICT 56..58
FT /note="DDN -> NND (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..77
FT /note="DQFLYFDLI -> NEFFDLIYL (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 128..130
FT /note="DIN -> NID (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..135
FT /note="QTD -> ENT (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..150
FT /note="NG -> GN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="Y -> YY (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 185..186
FT /note="QE -> EQ (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 246..247
FT /note="DN -> ND (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:3SEB"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3SEB"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:3SEB"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1SEB"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3SEB"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3SEB"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:3SEB"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:1SE4"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3SEB"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4C56"
FT STRAND 152..165
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 168..183
FT /evidence="ECO:0007829|PDB:3SEB"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1D5X"
FT STRAND 208..218
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3SEB"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:3SEB"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3SEB"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:3SEB"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:3SEB"
SQ SEQUENCE 266 AA; 31436 MW; B6D417F61CF018B0 CRC64;
MYKRLFISHV ILIFALILVI STPNVLAESQ PDPKPDELHK SSKFTGLMEN MKVLYDDNHV
SAINVKSIDQ FLYFDLIYSI KDTKLGNYDN VRVEFKNKDL ADKYKDKYVD VFGANYYYQC
YFSKKTNDIN SHQTDKRKTC MYGGVTEHNG NQLDKYRSIT VRVFEDGKNL LSFDVQTNKK
KVTAQELDYL TRHYLVKNKK LYEFNNSPYE TGYIKFIENE NSFWYDMMPA PGDKFDQSKY
LMMYNDNKMV DSKDVKIEVY LTTKKK
