From AureoWiki
Jump to navigation Jump to search

NCBI: 10-JUN-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0746 [new locus tag: SACOL_RS03830 ]
  • pan locus tag?: SAUPAN002570000
  • symbol: norR
  • pan gene symbol?: mgrA
  • synonym:
  • product: MarR family transcriptional regulator

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0746 [new locus tag: SACOL_RS03830 ]
  • symbol: norR
  • product: MarR family transcriptional regulator
  • replicon: chromosome
  • strand: -
  • coordinates: 767869..768312
  • length: 444
  • 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
    ATGTCTGATCAACATAATTTAAAAGAACAGCTATGCTTTAGTTTGTACAATGCTCAAAGA
    CAAGTTAATCGCTACTACTCTAACAAAGTTTTTAAGAAGTACAATCTAACATACCCACAA
    TTTCTTGTCTTAACAATTTTATGGGATGAATCTCCTGTAAACGTCAAGAAAGTCGTAACT
    GAATTAGCACTCGATACTGGTACAGTATCACCATTATTAAAACGAATGGAACAAGTAGAC
    TTAATTAAGCGTGAACGTTCCGAAGTCGATCAACGTGAAGTATTTATTCACTTGACTGAC
    AAAAGTGAAACTATTAGACCAGAATTAAGTAATGCATCTGACAAAGTCGCTTCAGCTTCT
    TCTTTATCGCAAGATGAAGTTAAAGAACTTAATCGCTTATTAGGTAAAGTCATTCATGCA
    TTTGATGAAACAAAGGAAAAATAA
    60
    120
    180
    240
    300
    360
    420
    444

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SACOL0746 [new locus tag: SACOL_RS03830 ]
  • symbol: NorR
  • description: MarR family transcriptional regulator
  • length: 147
  • theoretical pI: 7.59928
  • theoretical MW: 17089.3
  • GRAVY: -0.564626

Function[edit | edit source]

  • TIGRFAM:
    mobile rSAM pair MarR family regulator (TIGR04472; HMM-score: 54.1)
    homoprotocatechuate degradation operon regulator, HpaR (TIGR02337; HMM-score: 51.6)
    Signal transduction Regulatory functions DNA interactions staphylococcal accessory regulator family (TIGR01889; HMM-score: 47.2)
  • TheSEED  :
    • Transcriptional regulator MgrA (Regulator of autolytic activity)
  • PFAM:
    HTH (CL0123) MarR; MarR family (PF01047; HMM-score: 53.9)
    and 6 more
    HTH_27; Winged helix DNA-binding domain (PF13463; HMM-score: 33.1)
    Penicillinase_R; Penicillinase repressor (PF03965; HMM-score: 25.8)
    MarR_2; MarR family (PF12802; HMM-score: 24.1)
    TrmB; Sugar-specific transcriptional regulator TrmB (PF01978; HMM-score: 18.6)
    PadR; Transcriptional regulator PadR-like family (PF03551; HMM-score: 14.6)
    HTH_20; Helix-turn-helix domain (PF12840; HMM-score: 12.8)

Structure, modifications & cofactors[edit | edit source]

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

Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.67
    • Cytoplasmic Membrane Score: 0.01
    • Cellwall Score: 0.15
    • Extracellular Score: 0.17
    • 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): 0.003607
    • TAT(Tat/SPI): 0.000183
    • LIPO(Sec/SPII): 0.000845
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MSDQHNLKEQLCFSLYNAQRQVNRYYSNKVFKKYNLTYPQFLVLTILWDESPVNVKKVVTELALDTGTVSPLLKRMEQVDLIKRERSEVDQREVFIHLTDKSETIRPELSNASDKVASASSLSQDEVKELNRLLGKVIHAFDETKEK

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 2620 [5]
  • interaction partners:
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL02123-hydroxyacyl-CoA dehydrogenase  [6] (data from MRSA252)

Expression & Regulation[edit | edit source]

Operon[edit | edit source]

Regulation[edit | edit source]

Transcription pattern[edit | edit source]

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

Protein stability[edit | edit source]

  • half-life: 14.32 h [7]

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. 6.0 6.1 6.2 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)
  7. 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]