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 02-SEP-2026, entry version 160. DE RecName: Full=Enterotoxin type B; DE AltName: Full=SEB; DE Flags: Precursor; GN Name=entB; OS Staphylococcus aureus. OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; 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). Also causes 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:25015819, PubMed:8152483). CC Interacts with T-cell receptor beta variable 19/TRBV19 CC (PubMed:25015819, PubMed:9881971). {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M11118; AAA88550.1; -; Genomic_DNA. DR PIR; S27360; ENSAB6. DR RefSeq; WP_000278085.1; NZ_BAABQY010000006.1. 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 PDB; 8YBL; X-ray; 2.33 A; A=28-266. DR PDB; 8YBM; X-ray; 2.04 A; A/C=28-266. DR PDB; 8YBN; X-ray; 2.18 A; A=28-266. DR PDB; 8YBO; X-ray; 1.59 A; A/C=28-266. DR PDB; 8YBP; X-ray; 2.08 A; A=28-266. DR PDB; 8YKT; X-ray; 2.04 A; A=28-266. 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 ABCD; P01552; 52 sequenced antibodies. DR EvolutionaryTrace; P01552; -. DR PHI-base; PHI:10741; -. DR PRO; PR:P01552; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0090729; F:toxin activity; IEA:InterPro. DR Gene3D; 2.40.50.110; -; 1. DR Gene3D; 3.10.20.120; -; 1. 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; Bacterial enterotoxins; 1. DR SUPFAM; SSF54334; Superantigen toxins, C-terminal domain; 1. DR PROSITE; PS00277; STAPH_STREP_TOXIN_1; 1. DR PROSITE; PS00278; STAPH_STREP_TOXIN_2; 1. 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 PDBsum; 8YBL; -. DR PDBsum; 8YBM; -. DR PDBsum; 8YBN; -. DR PDBsum; 8YBO; -. DR PDBsum; 8YBP; -. DR PDBsum; 8YKT; -. 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 HELIX 30..32 FT /evidence="ECO:0007829|PDB:3SEB" FT STRAND 33..36 FT /evidence="ECO:0007829|PDB:3SEB" FT HELIX 37..40 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 68..71 FT /evidence="ECO:0007829|PDB:8YBP" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:8YBP" 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 TURN 204..206 FT /evidence="ECO:0007829|PDB:8YBN" 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 //