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P0A0L2

- ETXA_STAAU

UniProt

P0A0L2 - ETXA_STAAU

Protein

Enterotoxin type A

Gene

entA

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    Functioni

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

    Cofactori

    Binds 1 zinc ion per subunit. The zinc ion is necessary for the toxin interaction with MHC class II.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi211 – 2111Zinc
    Metal bindingi249 – 2491Zinc
    Metal bindingi251 – 2511Zinc

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. MHC class II protein binding Source: BHF-UCL

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Enterotoxin, Superantigen, Toxin

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enterotoxin type A
    Alternative name(s):
    SEA
    Gene namesi
    Name:entA
    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

    Allergomei2139. Sta a SEA.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 257233Enterotoxin type APRO_0000035604Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi120 ↔ 130

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    DIPiDIP-58974N.

    Structurei

    Secondary structure

    1
    257
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 314
    Helixi33 – 353
    Helixi39 – 413
    Helixi46 – 5510
    Beta strandi59 – 657
    Beta strandi72 – 787
    Beta strandi84 – 874
    Beta strandi89 – 946
    Helixi98 – 1047
    Beta strandi109 – 1146
    Helixi117 – 1193
    Beta strandi122 – 1243
    Helixi125 – 1273
    Beta strandi128 – 1336
    Beta strandi135 – 1373
    Turni139 – 1413
    Beta strandi142 – 1487
    Beta strandi151 – 1555
    Beta strandi158 – 1603
    Beta strandi166 – 17510
    Helixi176 – 19116
    Beta strandi193 – 1953
    Helixi197 – 1993
    Beta strandi205 – 2117
    Beta strandi213 – 2153
    Beta strandi218 – 2214
    Beta strandi227 – 2293
    Turni230 – 2323
    Helixi233 – 2375
    Beta strandi242 – 2443
    Beta strandi249 – 2557

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DYQX-ray1.50A25-257[»]
    1ESFX-ray1.90A/B25-257[»]
    1I4GX-ray2.10A/B25-257[»]
    1I4HX-ray2.90A/B25-257[»]
    1LO5X-ray3.20D25-257[»]
    1SEAmodel-A25-257[»]
    1SXTX-ray2.70A/B25-257[»]
    ProteinModelPortaliP0A0L2.
    SMRiP0A0L2. Positions 34-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A0L2.

    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.

    P0A0L2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKTAFTLLL FIALTLTTSP LVNGSEKSEE INEKDLRKKS ELQGTALGNL    50
    KQIYYYNEKA KTENKESHDQ FLQHTILFKG FFTDHSWYND LLVDFDSKDI 100
    VDKYKGKKVD LYGAYYGYQC AGGTPNKTAC MYGGVTLHDN NRLTEEKKVP 150
    INLWLDGKQN TVPLETVKTN KKNVTVQELD LQARRYLQEK YNLYNSDVFD 200
    GKVQRGLIVF HTSTEPSVNY DLFGAQGQYS NTLLRIYRDN KTINSENMHI 250
    DIYLYTS 257
    Length:257
    Mass (Da):29,669
    Last modified:February 15, 2005 - v1
    Checksum:iADEBF5BCA1F14677
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti242 – 2421T → S AA sequence (PubMed:3584106)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18970 Genomic DNA. Translation: AAA26681.1.
    PIRiA28664.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18970 Genomic DNA. Translation: AAA26681.1 .
    PIRi A28664.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DYQ X-ray 1.50 A 25-257 [» ]
    1ESF X-ray 1.90 A/B 25-257 [» ]
    1I4G X-ray 2.10 A/B 25-257 [» ]
    1I4H X-ray 2.90 A/B 25-257 [» ]
    1LO5 X-ray 3.20 D 25-257 [» ]
    1SEA model - A 25-257 [» ]
    1SXT X-ray 2.70 A/B 25-257 [» ]
    ProteinModelPortali P0A0L2.
    SMRi P0A0L2. Positions 34-257.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-58974N.

    Protein family/group databases

    Allergomei 2139. Sta a SEA.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P0A0L2.
    PROi P0A0L2.

    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 type A staphylococcal enterotoxin gene."
      Betley M.J., Mekalanos J.J.
      J. Bacteriol. 170:34-41(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FRI337.
    2. "Complete amino acid sequence of staphylococcal enterotoxin A."
      Huang I.-Y., Hughes J.L., Bergdoll M.S., Schantz E.J.
      J. Biol. Chem. 262:7006-7013(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-257.
    3. "Crystal structure of the superantigen staphylococcal enterotoxin type A."
      Schad E.M., Zaitseva I., Zaitsev V.N., Dohlsten M., Kalland T., Schlievert P.M., Ohlendorf D.H., Svensson L.A.
      EMBO J. 14:3292-3301(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    4. "The Co-crystal structure of staphylococcal enterotoxin type A with Zn2+ at 2.7-A resolution. Implications for major histocompatibility complex class II binding."
      Sundstroem M., Hallen D., Svensson A., Schad E., Dohlsten M., Abrahmsen L.
      J. Biol. Chem. 271:32212-32216(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    5. "Residues defining V beta specificity in staphylococcal enterotoxins."
      Swaminathan S., Furey W.F. Jr., Pletcher J., Sax M.
      Nat. Struct. Biol. 2:680-686(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    6. "A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity."
      Schad E.M., Papageorgiou A.C., Svensson L.A., Acharya K.R.
      J. Mol. Biol. 269:270-280(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPARISON OF STRUCTURE OF SEA AND SEC2.

    Entry informationi

    Entry nameiETXA_STAAU
    AccessioniPrimary (citable) accession number: P0A0L2
    Secondary accession number(s): P13163
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 50 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This toxin seems to be coded by a bacteriophage.

    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