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Revision as of 22:37, 10 March 2016 by AureoSysAdmin (talk | contribs) (Text replacement - "gene Genbank" to "gene RefSeq")
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Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_02125
  • symbol: SAOUHSC_02125
  • product: hypothetical protein
  • replicon: chromosome
  • strand: -
  • coordinates: 1999772..2000074
  • length: 303
  • essential: no DEG other strains

Accession numbers[edit | edit source]

  • Gene ID: 3921196 NCBI
  • RefSeq: YP_500616 NCBI

Phenotype[edit | edit source]

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

DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    ATGCAAATTGAAAAATTACGAGGTGCAGCGTTAGATGAATTGTTTGATGCAATACTAACG
    TTAGAAAATAGAGAAGAATGTTACCAATTTTTCGATGATTTGTGTACTGTAAATGAAATT
    CAATCACTGTCTCAAAGATTACAAGTTGCTAAAATGATTAAGCAAGGTTATACCTATGCA
    ACGATTGAACAAGAATCTGGAGCATCGACTGCAACGATTTCTAGAGTGAAGCGTTCATTA
    CAATGGGGTAATGATGCTTATACAATGATTTTAGATCGTATGAATATTGAAACAAATGAA
    TAA
    60
    120
    180
    240
    300
    303

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SAOUHSC_02125
  • symbol: SAOUHSC_02125
  • description: hypothetical protein
  • length: 100
  • theoretical pI: 4.27043
  • theoretical MW: 11518.9
  • GRAVY: -0.402

Function[edit | edit source]

  • TIGRFAM:
    Unknown function General TrpR homolog YerC/YecD (TIGR02531; HMM-score: 162.2)
    and 2 more
    Metabolism Amino acid biosynthesis Aromatic amino acid family trp operon repressor (TIGR01321; HMM-score: 20.8)
    Signal transduction Regulatory functions DNA interactions trp operon repressor (TIGR01321; HMM-score: 20.8)
  • TheSEED  :
    • His repressor
    CBSS-393121.3.peg.1913  His repressor
  • PFAM:
    HTH (CL0123) Trp_repressor; Trp repressor protein (PF01371; HMM-score: 117.4)
    and 4 more
    HTH_38; Helix-turn-helix domain (PF13936; HMM-score: 29.5)
    HTH_23; Homeodomain-like domain (PF13384; HMM-score: 19.5)
    HTH_36; Helix-turn-helix domain (PF13730; HMM-score: 14.5)
    HTH_7; Helix-turn-helix domain of resolvase (PF02796; HMM-score: 11.9)

Structure, modifications & interactions[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effector: Histidine
  • interaction partners:

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): 0.003872
    • TAT(Tat/SPI): 0.000703
    • LIPO(Sec/SPII): 0.000578
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

  • GI: 88195806 NCBI
  • UniProt: Q2G1Y1 UniProt
  • protein Genbank : _
  • RefSeq: YP_500616 NCBI

Protein sequence[edit | edit source]

  • MQIEKLRGAALDELFDAILTLENREECYQFFDDLCTVNEIQSLSQRLQVAKMIKQGYTYATIEQESGASTATISRVKRSLQWGNDAYTMILDRMNIETNE

Peptides[edit | edit source]

Expression & Regulation[edit | edit source]

Regulation[edit | edit source]

  • sigma factors : _
  • regulator: HisR* (repression) regulon
    HisR*(TF)important in Histidine biosynthesis; RegPrecise 

Transcription pattern[edit | edit source]

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

Stability[edit | edit source]

  • half-life: no data available

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. 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)
  2. 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)
  3. 3.0 3.1 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 | edit source]

Semen A Leyn, Marat D Kazanov, Natalia V Sernova, Ekaterina O Ermakova, Pavel S Novichkov, Dmitry A Rodionov
Genomic reconstruction of the transcriptional regulatory network in Bacillus subtilis.
J Bacteriol: 2013, 195(11);2463-73
[PubMed:23504016] [WorldCat.org] [DOI] (I p)