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NCBI: 03-AUG-2016

Summary[edit source | edit]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_01822
  • pan locus tag?: SAUPAN004365000
  • symbol: tpx
  • pan gene symbol?: tpx
  • synonym:
  • product: 2-Cys peroxiredoxin

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SAOUHSC_01822
  • symbol: tpx
  • product: 2-Cys peroxiredoxin
  • replicon: chromosome
  • strand: -
  • coordinates: 1727898..1728392
  • length: 495
  • essential: no DEG other strains

Accession numbers[edit source | edit]

Phenotype[edit source | edit]

  • Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    ATGACTGAAATAACATTCAAAGGTGGACCAATCCACTTAAAAGGTCAACAAATTAATGAA
    GGTGATTTTGCACCTGATTTTACAGTGTTAGATAATGACTTAAATCAAGTAACATTAGCA
    GATTATGCTGGTAAAAAGAAATTAATTAGTGTGGTACCATCAATTGATACAGGTGTTTGT
    GATCAGCAGACTCGCAAATTCAACTCTGATGCTTCTAAAGAAGAGGGGATTGTGCTTACA
    ATTTCAGCAGACTTACCATTCGCACAAAAAAGATGGTGCGCTTCAGCAGGTTTAGACAAT
    GTCATTACATTAAGTGACCACCGTGACTTATCATTTGGTGAAAACTATGGCGTTGTTATG
    GAAGAACTTCGCTTATTAGCTCGTGCAGTATTTGTATTAGATGCAGATAATAAAGTTGTT
    TATAAAGAAATCGTTAGTGAAGGTACTGATTTCCCAGATTTTGATGCTGCTTTAGCTGCA
    TACAAAAATATTTAA
    60
    120
    180
    240
    300
    360
    420
    480
    495

Protein[edit source | edit]

Protein Data Bank: 3P7X

General[edit source | edit]

  • locus tag: SAOUHSC_01822
  • symbol: Tpx
  • description: 2-Cys peroxiredoxin
  • length: 164
  • theoretical pI: 4.33649
  • theoretical MW: 18005.2
  • GRAVY: -0.134146

Function[edit source | edit]

  • reaction:
    EC 1.11.1.-?  ExPASy
  • TIGRFAM:
    Cellular processesCellular processesDetoxificationperoxiredoxin (TIGR03137; EC 1.11.1.15; HMM-score: 25.2)
    Cellular processesCellular processesAdaptations to atypical conditionsperoxiredoxin (TIGR03137; EC 1.11.1.15; HMM-score: 25.2)
  • TheSEED:  
    Sulfur MetabolismSulfur Metabolism - no subcategoryThioredoxin-disulfide reductase Thiol peroxidase, Tpx-type (EC 1.11.1.15) 
    CBSS-257314.1.peg.752 Thiol peroxidase, Tpx-type (EC 1.11.1.15) 
  • PFAM:
    Thioredoxin (CL0172) Redoxin; Redoxin (PF08534; HMM-score: 89.4)
    AhpC-TSA; AhpC/TSA family (PF00578; HMM-score: 64.6)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:

Localization[edit source | edit]

  • PSORTb: unknown (no significant prediction)
    • Cytoplasmic Score: 2.5
    • Cytoplasmic Membrane Score: 2.5
    • Cellwall Score: 2.5
    • Extracellular Score: 2.5
    • 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
    • Ymax: 0.111
    • Ymax_pos: 69
    • Cmax: 0.117
    • Cmax_pos: 25
    • Smax: 0.15
    • Smax_pos: 21
    • Smean: 0.092
    • D: 0.104
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MTEITFKGGPIHLKGQQINEGDFAPDFTVLDNDLNQVTLADYAGKKKLISVVPSIDTGVCDQQTRKFNSDASKEEGIVLTISADLPFAQKRWCASAGLDNVITLSDHRDLSFGENYGVVMEELRLLARAVFVLDADNKVVYKEIVSEGTDFPDFDAALAAYKNI

Experimental data[edit source | edit]

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: no data available

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  1. Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
    A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
    Sci Rep: 2017, 7(1);9718
    [PubMed:28887440] [WorldCat.org] [DOI] (I e)
  2. Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
    A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
    Proteomics: 2015, 15(21);3648-61
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  3. Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
    Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
    PLoS Genet.: 2016, 12(4);e1005962
    [PubMed:27035918] [WorldCat.org] [DOI] (I e)

Relevant publications[edit source | edit]

Sudipta Bhattacharyya, Debajyoti Dutta, Ananta Kumar Ghosh, Amit Kumar Das
Cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of an atypical two-cysteine peroxiredoxin (SAOUHSC_01822) from Staphylococcus aureus NCTC 8325.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.: 2009, 65(Pt 11);1113-5
[PubMed:19923729] [WorldCat.org] [DOI] (I p)