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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1794 [new locus tag: SACOL_RS09195 ]
  • pan locus tag?: SAUPAN004411000
  • symbol: SACOL1794
  • pan gene symbol?: —
  • synonym:
  • product: thioredoxin

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1794 [new locus tag: SACOL_RS09195 ]
  • symbol: SACOL1794
  • product: thioredoxin
  • replicon: chromosome
  • strand: -
  • coordinates: 1842545..1842856
  • length: 312
  • essential: unknown other strains

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    ATGAAACAACTTGAATCAGAACAACAATTTGAATCTTTAAAACAAGGTGCTACAGTATTT
    GAATTCACTGCAGGCTGGTGTCCAGATTGTAGAGTGATAGAACCAGATTTACCGGAATTA
    GAAGCGAGATATCCTATGTTTGACTTCGTATCAGTAGACCGTGATAAATTTATGGATATT
    TGTATTGAAAATGGTATTATGGGTATTCCAAGTTTTCTAGTATATAAAAATGGAGAACTG
    CTTGGAAGTTATATTGGAAAAGAACGAAAATCAATTGAACAGATAGATGCATTTTTAGCT
    CAATACGTGTAA
    60
    120
    180
    240
    300
    312

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1794 [new locus tag: SACOL_RS09195 ]
  • symbol: SACOL1794
  • description: thioredoxin
  • length: 103
  • theoretical pI: 4.14259
  • theoretical MW: 11855.5
  • GRAVY: -0.168932

⊟Function[edit | edit source]

  • TIGRFAM:
    Metabolism Energy metabolism Electron transport thioredoxin (TIGR01068; HMM-score: 47.6)
    and 6 more
    protein disulfide isomerase (TIGR01130; HMM-score: 26.4)
    Genetic information processing Protein fate Protein folding and stabilization protein disulfide-isomerase domain (TIGR01126; HMM-score: 24.9)
    Genetic information processing Protein fate Protein folding and stabilization periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily (TIGR00385; HMM-score: 19.2)
    glutaredoxin-like protein (TIGR02200; HMM-score: 16.2)
    glutaredoxin-like protein, YruB-family (TIGR02196; HMM-score: 14.6)
    Unknown function General redox-active disulfide protein 1 (TIGR00411; HMM-score: 13.1)
  • TheSEED  :
    • Thioredoxin-like protein YtpP
  • PFAM:
    Thioredoxin (CL0172) Thioredoxin; Thioredoxin (PF00085; HMM-score: 58.1)
    and 6 more
    Thioredoxin_9; Thioredoxin (PF14595; HMM-score: 23.9)
    Thioredoxin_8; Thioredoxin-like (PF13905; HMM-score: 17.6)
    Phosducin; Phosducin (PF02114; HMM-score: 16.2)
    Thioredoxin_2; Thioredoxin-like domain (PF13098; HMM-score: 15.3)
    Thioredoxin_4; Thioredoxin (PF13462; HMM-score: 12.5)
    DSBA; DSBA-like thioredoxin domain (PF01323; HMM-score: 11.8)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • Internal Helices: 0
  • LocateP: Intracellular
    • Prediction by SwissProt Classification: Cytoplasmic
    • Pathway Prediction: No pathway
    • Intracellular possibility: 1
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: 1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.013564
    • TAT(Tat/SPI): 0.002238
    • LIPO(Sec/SPII): 0.007556
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKQLESEQQFESLKQGATVFEFTAGWCPDCRVIEPDLPELEARYPMFDFVSVDRDKFMDICIENGIMGIPSFLVYKNGELLGSYIGKERKSIEQIDAFLAQYV

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 2656 [4]
  • interaction partners:
    SACOL1637(dnaK)molecular chaperone DnaK  [5] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [5] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [5] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [5] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: 28.51 h [6]

⊟Biological Material[edit | edit source]

⊟Mutants[edit | edit source]

⊟Expression vector[edit | edit source]

⊟lacZ fusion[edit | edit source]

⊟GFP fusion[edit | edit source]

⊟two-hybrid system[edit | edit source]

⊟FLAG-tag construct[edit | edit source]

⊟Antibody[edit | edit source]

⊟Other Information[edit | edit source]

You are kindly invited to share additional interesting facts.

⊟Literature[edit | edit source]

⊟References[edit | edit source]

  1. ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
    A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
    PLoS One: 2009, 4(12);e8176
    [PubMed:19997597] [WorldCat.org] [DOI] (I e)
  2. ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
    Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
    J Proteome Res: 2011, 10(4);1657-66
    [PubMed:21323324] [WorldCat.org] [DOI] (I p)
  3. ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
    The Staphylococcus aureus proteome.
    Int J Med Microbiol: 2014, 304(2);110-20
    [PubMed:24439828] [WorldCat.org] [DOI] (I p)
  4. ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
    Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
    Sci Rep: 2016, 6;28172
    [PubMed:27344979] [WorldCat.org] [DOI] (I e)
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
    Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
    J Proteome Res: 2011, 10(3);1139-50
    [PubMed:21166474] [WorldCat.org] [DOI] (I p)
  6. ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
    Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
    Mol Cell Proteomics: 2012, 11(9);558-70
    [PubMed:22556279] [WorldCat.org] [DOI] (I p)

⊟Relevant publications[edit | edit source]

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