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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2055 [new locus tag: SACOL_RS10755 ]
  • pan locus tag?: SAUPAN005334000
  • symbol: rsbW
  • pan gene symbol?: rsbW
  • synonym:
  • product: serine-protein kinase RsbW

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2055 [new locus tag: SACOL_RS10755 ]
  • symbol: rsbW
  • product: serine-protein kinase RsbW
  • replicon: chromosome
  • strand: -
  • coordinates: 2121937..2122416
  • length: 480
  • 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
    361
    421
    ATGCAATCTAAAGAAGATTTTATCGAAATGCGCGTGCCAGCATCGGCAGAGTATGTAAGT
    TTAATTCGTTTAACACTTTCTGGCGTTTTTTCGAGAGCTGGTGCTACATATGATGATATT
    GAAGATGCCAAGATTGCAGTTAGTGAAGCTGTGACAAATGCAGTTAAACATGCATACAAA
    GAAAATAACAATGTGGGCATTATTAACATATATTTTGAAATTTTAGAAGATAAAATTAAA
    ATTGTTATTTCTGATAAAGGTGACAGTTTTGATTATGAAACAACTAAATCAAAAATAGGT
    CCTTACGATAAAGACGAAAATATAGACTTTTTACGCGAAGGTGGCCTAGGTTTATTTTTA
    ATCGAATCTTTAATGGATGAAGTCACAGTATATAAAGAATCTGGTGTGACAATCAGTATG
    ACTAAGTATATAAAAAAAGAGCAGGTGCGAAATAATGGCGAAAGAGTCGAAATCAGCTAA
    60
    120
    180
    240
    300
    360
    420
    480

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2055 [new locus tag: SACOL_RS10755 ]
  • symbol: RsbW
  • description: serine-protein kinase RsbW
  • length: 159
  • theoretical pI: 4.45015
  • theoretical MW: 17921.1
  • GRAVY: -0.308176

⊟Function[edit | edit source]

  • reaction:
    EC 2.7.11.1?  ExPASy
    Non-specific serine/threonine protein kinase ATP + a protein = ADP + a phosphoprotein
  • TIGRFAM:
    anti-sigma B factor (TIGR01924; EC 2.7.11.1; HMM-score: 272.2)
    and 2 more
    Cellular processes Cellular processes Sporulation and germination anti-sigma F factor (TIGR01925; EC 2.7.11.1; HMM-score: 63.8)
    Signal transduction Regulatory functions Protein interactions anti-sigma F factor (TIGR01925; EC 2.7.11.1; HMM-score: 63.8)
  • TheSEED  :
    • Serine-protein kinase RsbW (EC 2.7.11.1)
    Stress Response Stress Response - no subcategory SigmaB stress responce regulation  Serine-protein kinase rsbW (EC 2.7.11.1)
  • PFAM:
    His_Kinase_A (CL0025) HATPase_c_2; Histidine kinase-like ATPase domain (PF13581; HMM-score: 94.7)
    and 1 more
    HATPase_c; Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase (PF02518; HMM-score: 26.2)

⊟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): 0.085882
    • TAT(Tat/SPI): 0.053039
    • LIPO(Sec/SPII): 0.006369
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDFLREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1883 [5]
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: SigB* (activation) regulon
    SigB*(sigma factor)controlling a large regulon involved in stress/starvation response and adaptation;  [6] [7]   other strains

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 42.48 h [8]

⊟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, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J Proteome Res: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 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)
  6. ↑ Markus Bischoff, Paul Dunman, Jan Kormanec, Daphne Macapagal, Ellen Murphy, William Mounts, Brigitte Berger-Bächi, Steven Projan
    Microarray-based analysis of the Staphylococcus aureus sigmaB regulon.
    J Bacteriol: 2004, 186(13);4085-99
    [PubMed:15205410] [WorldCat.org] [DOI] (P p)
  7. ↑ Jan Pané-Farré, Beate Jonas, Konrad Förstner, Susanne Engelmann, Michael Hecker
    The sigmaB regulon in Staphylococcus aureus and its regulation.
    Int J Med Microbiol: 2006, 296(4-5);237-58
    [PubMed:16644280] [WorldCat.org] [DOI] (P p)
  8. ↑ 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]

S Wu, H de Lencastre, A Tomasz
Sigma-B, a putative operon encoding alternate sigma factor of Staphylococcus aureus RNA polymerase: molecular cloning and DNA sequencing.
J Bacteriol: 1996, 178(20);6036-42
[PubMed:8830703] [WorldCat.org] [DOI] (P p)

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