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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_02155
  • pan locus tag?: SAUPAN005000000
  • symbol: SAOUHSC_02155
  • pan gene symbol?: pmtR
  • synonym:
  • product: hypothetical protein

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_02155
  • symbol: SAOUHSC_02155
  • product: hypothetical protein
  • replicon: chromosome
  • strand: -
  • coordinates: 2026331..2026711
  • length: 381
  • essential: no [1] DEG 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
    361
    ATGAAAATAATTTTAAAAAACAATAGTGATTTTCCGATTTATGAACAGATTAAGCAACAA
    GTAAAACAAAATATTTTAAAGGGACATGTTGCTCCTGGAGAGCATTTGCCGTCAATGAGA
    GAACTTGCCAAAGATCTTCAAGTAAGTTTGATTACTACCAAACGTGCTTATGAAGATTTA
    GAGAAAGACGGTTTTGTTACAACAATTAGAGGAAAAGGGACCTTTGTTAAGGAGCAAGAT
    AGTTCTATTTTAAAAGAGAAACAATTTTTTACCATTGAAAATTTGGTTAAAGAATTGGTT
    AATGAAGCGCAAGCCATCGAAATGTCACTTGAGGAACTGCAGGATATTTTAACGTTCATT
    TATGAGGAGGAATCATCATGA
    60
    120
    180
    240
    300
    360
    381

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SAOUHSC_02155
  • symbol: SAOUHSC_02155
  • description: hypothetical protein
  • length: 126
  • theoretical pI: 4.70971
  • theoretical MW: 14532.5
  • GRAVY: -0.430952

⊟Function[edit | edit source]

  • TIGRFAM:
    Metabolism Energy metabolism Amino acids and amines histidine utilization repressor (TIGR02018; HMM-score: 59.3)
    Signal transduction Regulatory functions DNA interactions histidine utilization repressor (TIGR02018; HMM-score: 59.3)
    and 15 more
    Metabolism Transport and binding proteins Anions phosphonate metabolism transcriptional regulator PhnF (TIGR02325; HMM-score: 45.2)
    Signal transduction Regulatory functions DNA interactions phosphonate metabolism transcriptional regulator PhnF (TIGR02325; HMM-score: 45.2)
    Signal transduction Regulatory functions DNA interactions trehalose operon repressor (TIGR02404; HMM-score: 43.6)
    Signal transduction Regulatory functions DNA interactions phosphonate utilization transcriptional regulator PhnR (TIGR03337; HMM-score: 35.1)
    phosphonate utilization associated transcriptional regulator (TIGR03338; HMM-score: 32.7)
    Signal transduction Regulatory functions DNA interactions CRISPR locus-related DNA-binding protein (TIGR01884; HMM-score: 23.8)
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis fatty acid metabolism transcriptional regulator FadR (TIGR02812; HMM-score: 23.1)
    Metabolism Fatty acid and phospholipid metabolism Degradation fatty acid metabolism transcriptional regulator FadR (TIGR02812; HMM-score: 23.1)
    Signal transduction Regulatory functions DNA interactions fatty acid metabolism transcriptional regulator FadR (TIGR02812; HMM-score: 23.1)
    Unknown function General Rrf2 family protein (TIGR00738; HMM-score: 13.5)
    putative choline sulfate-utilization transcription factor (TIGR03418; HMM-score: 13.5)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other iron-sulfur cluster biosynthesis transcriptional regulator SufR (TIGR02702; HMM-score: 13)
    Signal transduction Regulatory functions DNA interactions iron-sulfur cluster biosynthesis transcriptional regulator SufR (TIGR02702; HMM-score: 13)
    Genetic information processing DNA metabolism DNA replication, recombination, and repair repressor LexA (TIGR00498; EC 3.4.21.88; HMM-score: 12.8)
    Signal transduction Regulatory functions DNA interactions repressor LexA (TIGR00498; EC 3.4.21.88; HMM-score: 12.8)
  • TheSEED  :
    • Transcriptional regulator SAV1934, YtrA family
  • PFAM:
    HTH (CL0123) GntR; Bacterial regulatory proteins, gntR family (PF00392; HMM-score: 64.4)
    and 10 more
    HTH_24; Winged helix-turn-helix DNA-binding (PF13412; HMM-score: 19.3)
    Rrf2; Transcriptional regulator (PF02082; HMM-score: 19.2)
    HTH_41; Helix-turn-helix domain (PF14502; HMM-score: 18.3)
    no clan defined Syntaxin-6_N; Syntaxin 6, N-terminal (PF09177; HMM-score: 13.7)
    HTH (CL0123) RPA_C; Replication protein A C terminal (PF08784; HMM-score: 13.1)
    MarR_2; MarR family (PF12802; HMM-score: 13)
    MarR; MarR family (PF01047; HMM-score: 12.9)
    LexA_DNA_bind; LexA DNA binding domain (PF01726; HMM-score: 12.8)
    HTH_11; HTH domain (PF08279; HMM-score: 12.2)
    HTH_36; Helix-turn-helix domain (PF13730; HMM-score: 12.1)

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

  • domains:
  • modifications:
  • cofactors:
  • effectors: Phenol-soluble modulins (PSMs) [2]
  • genes regulated by PmtR*, TF important in Hypothetical ABC transporterRegPrecise
    repression
    pmtD* < pmtC* < pmtB* < pmtA* < pmtR*
    transcription unit transferred from N315 data RegPrecise

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • 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): 0.003235
    • TAT(Tat/SPI): 0.000192
    • LIPO(Sec/SPII): 0.000299
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKIILKNNSDFPIYEQIKQQVKQNILKGHVAPGEHLPSMRELAKDLQVSLITTKRAYEDLEKDGFVTTIRGKGTFVKEQDSSILKEKQFFTIENLVKELVNEAQAIEMSLEELQDILTFIYEEESS

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [3] [4]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell:
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: PmtR* (repression) regulon
    PmtR*(TF)important in Hypothetical ABC transporter; RegPrecise 

⊟Transcription pattern[edit | edit source]

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

⊟Protein 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. ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
    Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
    BMC Genomics: 2009, 10;291
    [PubMed:19570206] [WorldCat.org] [DOI] (I e)
  2. ↑ Hwang-Soo Joo, Michael Otto
    Toxin-mediated gene regulatory mechanism in Staphylococcus aureus.
    Microb Cell: 2016, 4(1);29-31
    [PubMed:28357385] [WorldCat.org] [DOI] (P e)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 5.0 5.1 5.2 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]

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