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P01552

- ETXB_STAAU

UniProt

P01552 - ETXB_STAAU

Protein

Enterotoxin type B

Gene

entB

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death.

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Enterotoxin, Superantigen, Toxin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enterotoxin type B
    Alternative name(s):
    SEB
    Gene namesi
    Name:entB
    OrganismiStaphylococcus aureus
    Taxonomic identifieri1280 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Protein family/group databases

    Allergomei2140. Sta a SEB.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 266239Enterotoxin type BPRO_0000035606Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi120 ↔ 140

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-35541N.
    IntActiP01552. 1 interaction.

    Structurei

    Secondary structure

    1
    266
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 364
    Helixi41 – 433
    Helixi49 – 524
    Helixi53 – 553
    Beta strandi60 – 667
    Beta strandi67 – 693
    Beta strandi75 – 784
    Turni83 – 853
    Beta strandi89 – 946
    Helixi98 – 1047
    Beta strandi107 – 1137
    Turni128 – 1314
    Beta strandi138 – 1425
    Beta strandi145 – 1484
    Turni149 – 1513
    Beta strandi152 – 16514
    Beta strandi168 – 18316
    Helixi184 – 19916
    Beta strandi204 – 2063
    Beta strandi208 – 21811
    Beta strandi221 – 2266
    Beta strandi231 – 2333
    Helixi237 – 2415
    Helixi242 – 2465
    Beta strandi249 – 2513
    Turni252 – 2543
    Beta strandi255 – 2639

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D5MX-ray2.00C28-266[»]
    1D5XX-ray2.45C28-266[»]
    1D5ZX-ray2.00C28-266[»]
    1D6EX-ray2.45C28-266[»]
    1GOZX-ray2.00A/B28-266[»]
    1SBBX-ray2.40B/D28-266[»]
    1SE3X-ray2.30A28-266[»]
    1SE4X-ray1.90A28-266[»]
    1SEBX-ray2.70D/H29-262[»]
    2SEBX-ray2.50D28-266[»]
    3GP7X-ray1.90A/B28-266[»]
    3R8BX-ray2.95A/C/E/G/I/K/M/O28-266[»]
    3SEBX-ray1.48A28-265[»]
    3W2DX-ray3.10A28-266[»]
    ProteinModelPortaliP01552.
    SMRiP01552. Positions 28-266.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01552.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.10.20.120. 1 hit.
    InterProiIPR008992. Enterotoxin.
    IPR006126. Staph/Strept_toxin_CS.
    IPR006173. Staph_tox_OB.
    IPR016091. SuperAg_toxin_C.
    IPR013307. Superantigen_bac.
    IPR006123. Toxin_b-grasp_Staph/Strep.
    IPR006177. Toxin_bac.
    [Graphical view]
    PfamiPF02876. Stap_Strp_tox_C. 1 hit.
    PF01123. Stap_Strp_toxin. 1 hit.
    [Graphical view]
    PRINTSiPR00279. BACTRLTOXIN.
    PR01898. SAGSUPRFAMLY.
    SUPFAMiSSF50203. SSF50203. 1 hit.
    SSF54334. SSF54334. 1 hit.
    PROSITEiPS00277. STAPH_STREP_TOXIN_1. 1 hit.
    PS00278. STAPH_STREP_TOXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P01552-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYKRLFISHV ILIFALILVI STPNVLAESQ PDPKPDELHK SSKFTGLMEN    50
    MKVLYDDNHV SAINVKSIDQ FLYFDLIYSI KDTKLGNYDN VRVEFKNKDL 100
    ADKYKDKYVD VFGANYYYQC YFSKKTNDIN SHQTDKRKTC MYGGVTEHNG 150
    NQLDKYRSIT VRVFEDGKNL LSFDVQTNKK KVTAQELDYL TRHYLVKNKK 200
    LYEFNNSPYE TGYIKFIENE NSFWYDMMPA PGDKFDQSKY LMMYNDNKMV 250
    DSKDVKIEVY LTTKKK 266
    Length:266
    Mass (Da):31,436
    Last modified:August 13, 1987 - v1
    Checksum:iB6D417F61CF018B0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 583DDN → NND AA sequence (PubMed:5470821)Curated
    Sequence conflicti69 – 779DQFLYFDLI → NEFFDLIYL AA sequence (PubMed:5470821)Curated
    Sequence conflicti118 – 1181Missing AA sequence (PubMed:5470821)Curated
    Sequence conflicti128 – 1303DIN → NID AA sequence (PubMed:5470821)Curated
    Sequence conflicti133 – 1353QTD → ENT AA sequence (PubMed:5470821)Curated
    Sequence conflicti149 – 1502NG → GN AA sequence (PubMed:5470821)Curated
    Sequence conflicti156 – 1561Y → YY AA sequence (PubMed:5470821)Curated
    Sequence conflicti185 – 1862QE → EQ AA sequence (PubMed:5470821)Curated
    Sequence conflicti233 – 2331D → N AA sequence (PubMed:5470821)Curated
    Sequence conflicti246 – 2472DN → ND AA sequence (PubMed:5470821)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11118 Genomic DNA. Translation: AAA88550.1.
    PIRiS27360. ENSAB6.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11118 Genomic DNA. Translation: AAA88550.1 .
    PIRi S27360. ENSAB6.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D5M X-ray 2.00 C 28-266 [» ]
    1D5X X-ray 2.45 C 28-266 [» ]
    1D5Z X-ray 2.00 C 28-266 [» ]
    1D6E X-ray 2.45 C 28-266 [» ]
    1GOZ X-ray 2.00 A/B 28-266 [» ]
    1SBB X-ray 2.40 B/D 28-266 [» ]
    1SE3 X-ray 2.30 A 28-266 [» ]
    1SE4 X-ray 1.90 A 28-266 [» ]
    1SEB X-ray 2.70 D/H 29-262 [» ]
    2SEB X-ray 2.50 D 28-266 [» ]
    3GP7 X-ray 1.90 A/B 28-266 [» ]
    3R8B X-ray 2.95 A/C/E/G/I/K/M/O 28-266 [» ]
    3SEB X-ray 1.48 A 28-265 [» ]
    3W2D X-ray 3.10 A 28-266 [» ]
    ProteinModelPortali P01552.
    SMRi P01552. Positions 28-266.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35541N.
    IntActi P01552. 1 interaction.

    Protein family/group databases

    Allergomei 2140. Sta a SEB.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P01552.
    PROi P01552.

    Family and domain databases

    Gene3Di 3.10.20.120. 1 hit.
    InterProi IPR008992. Enterotoxin.
    IPR006126. Staph/Strept_toxin_CS.
    IPR006173. Staph_tox_OB.
    IPR016091. SuperAg_toxin_C.
    IPR013307. Superantigen_bac.
    IPR006123. Toxin_b-grasp_Staph/Strep.
    IPR006177. Toxin_bac.
    [Graphical view ]
    Pfami PF02876. Stap_Strp_tox_C. 1 hit.
    PF01123. Stap_Strp_toxin. 1 hit.
    [Graphical view ]
    PRINTSi PR00279. BACTRLTOXIN.
    PR01898. SAGSUPRFAMLY.
    SUPFAMi SSF50203. SSF50203. 1 hit.
    SSF54334. SSF54334. 1 hit.
    PROSITEi PS00277. STAPH_STREP_TOXIN_1. 1 hit.
    PS00278. STAPH_STREP_TOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the enterotoxin B gene from Staphylococcus aureus."
      Jones C.L., Khan S.A.
      J. Bacteriol. 166:29-33(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Molecular cloning of staphylococcal enterotoxin B gene in Escherichia coli and Staphylococcus aureus."
      Ranelli D.M., Jones C.L., Johns M.B., Mussey G.J., Khan S.A.
      Proc. Natl. Acad. Sci. U.S.A. 82:5850-5854(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-91.
    3. "The primary structure of staphylococcal enterotoxin B. 3. The cyanogen bromide peptides of reduced and aminoethylated enterotoxin B, and the complete amino acid sequence."
      Huang I.-Y., Bergdoll M.S.
      J. Biol. Chem. 245:3518-3525(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-266 (S-6).
    4. "Crystal structure of staphylococcal enterotoxin B, a superantigen."
      Swaminathan S., Furey W.F. Jr., Pletcher J., Sax M.
      Nature 359:801-806(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    5. "Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen."
      Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., Chi Y.I., Stauffacher C., Strominger J.L., Wiley D.C.
      Nature 368:711-718(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH MHC II.
    6. "Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B."
      Li H., Llera A., Tsuchiya D., Leder L., Ysern X., Schlievert P.M., Karjalainen K., Mariuzza R.A.
      Immunity 9:807-816(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH TCR.
    7. "Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5-A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors."
      Papageorgiou A.C., Tranter H.S., Acharya K.R.
      J. Mol. Biol. 277:61-79(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

    Entry informationi

    Entry nameiETXB_STAAU
    AccessioniPrimary (citable) accession number: P01552
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3