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NCBI: 10-JUN-2013

Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0539 [new locus tag: SACOL_RS02755 ]
  • pan locus tag?: SAUPAN002234000
  • symbol: purR
  • pan gene symbol?: purR
  • synonym:
  • product: pur operon repressor

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0539 [new locus tag: SACOL_RS02755 ]
  • symbol: purR
  • product: pur operon repressor
  • replicon: chromosome
  • strand: +
  • coordinates: 547963..548787
  • length: 825
  • 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
    481
    541
    601
    661
    721
    781
    ATGAGATATAAACGAAGCGAGAGAATTGTTTTTATGACGCAATATTTGATGAACCATCCG
    AATAAATTGATTCCATTAACTTTTTTTGTGAAAAAATTTAAACAGGCGAAGTCTTCAATA
    AGTGAAGATGTCCAAATTATAAAAAATACATTCCAAAAAGAAAAGTTAGGTACAGTAATT
    ACTACTGCTGGCGCAAGTGGTGGTGTTACGTATAAACCAATGATGAGTAAAGAAGAGGCG
    ACTGAAGTTGTTAATGAGGTCATTACTCTATTAGAAGAGAAAGAACGTTTGTTACCTGGC
    GGATATTTATTTTTATCAGATTTGGTAGGTAATCCATCGCTACTAAACAAAGTTGGTAAG
    TTAATTGCCAGTATTTACATGGAAGAAAAATTAGATGCTGTTGTTACCATTGCGACAAAA
    GGTATTTCATTGGCAAATGCGGTTGCTAATATTTTAAATTTACCAGTAGTAGTGATTAGA
    AAAGACAACAAGGTGACTGAAGGTTCTACAGTTTCAATTAATTACGTTTCAGGATCTTCA
    AGAAAAATAGAAACAATGGTACTTTCGAAGAGAACTTTAGCAGAAAATTCAAATGTTTTA
    GTTGTCGATGATTTTATGAGGGCTGGTGGCTCTATTAATGGTGTTATGAATTTAATGAAT
    GAGTTTAAAGCCCATGTAAAAGGGGTATCAGTACTTGTAGAATCAAAAGAAGTTAAACAA
    AGATTGATTGAAGATTATACTTCCTTAGTGAAATTATCTGATGTAGATGAATATAATCAA
    GAGTTTAACGTAGAACCTGGCAACAGTTTATCTAAGTTTTCATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    825

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SACOL0539 [new locus tag: SACOL_RS02755 ]
  • symbol: PurR
  • description: pur operon repressor
  • length: 274
  • theoretical pI: 9.54206
  • theoretical MW: 30395.1
  • GRAVY: -0.0715328

Function[edit | edit source]

  • TIGRFAM:
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis pur operon repressor PurR (TIGR01743; HMM-score: 361.7)
    Signal transduction Regulatory functions DNA interactions pur operon repressor PurR (TIGR01743; HMM-score: 361.7)
    and 6 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides xanthine phosphoribosyltransferase (TIGR01744; EC 2.4.2.22; HMM-score: 67)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides adenine phosphoribosyltransferase (TIGR01090; EC 2.4.2.7; HMM-score: 65.1)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis orotate phosphoribosyltransferase (TIGR00336; EC 2.4.2.10; HMM-score: 43.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis orotate phosphoribosyltransferase (TIGR01367; EC 2.4.2.10; HMM-score: 30.3)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis ribose-phosphate diphosphokinase (TIGR01251; EC 2.7.6.1; HMM-score: 20)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides hypoxanthine phosphoribosyltransferase (TIGR01203; EC 2.4.2.8; HMM-score: 18.1)
  • TheSEED  :
    • Pur operon repressor PurR
    Nucleosides and Nucleotides Purines De Novo Purine Biosynthesis  PurR: transcription regulator associated with purine metabolism
  • PFAM:
    HTH (CL0123) PuR_N; Bacterial purine repressor, N-terminal (PF09182; HMM-score: 107.4)
    and 1 more
    PRTase-like (CL0533) Pribosyltran; Phosphoribosyl transferase domain (PF00156; HMM-score: 76.7)

Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • genes regulated by PurR, TF important in Purine metabolism: in N315

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: 0.67
    • Signal peptide possibility: -0.5
    • N-terminally Anchored Score: 1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.040109
    • TAT(Tat/SPI): 0.000536
    • LIPO(Sec/SPII): 0.001557
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MRYKRSERIVFMTQYLMNHPNKLIPLTFFVKKFKQAKSSISEDVQIIKNTFQKEKLGTVITTAGASGGVTYKPMMSKEEATEVVNEVITLLEEKERLLPGGYLFLSDLVGNPSLLNKVGKLIASIYMEEKLDAVVTIATKGISLANAVANILNLPVVVIRKDNKVTEGSTVSINYVSGSSRKIETMVLSKRTLAENSNVLVVDDFMRAGGSINGVMNLMNEFKAHVKGVSVLVESKEVKQRLIEDYTSLVKLSDVDEYNQEFNVEPGNSLSKFS

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Signal peptide containing [1] [2] [3]
  • quantitative data / protein copy number per cell: 537 [4]
  • interaction partners:
    SACOL1215(carB)carbamoyl phosphate synthase large subunit  [5] (data from MRSA252)
    SACOL1016(fabI)enoyl-ACP reductase  [5] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [5] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [5] (data from MRSA252)
    SACOL1961(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [5] (data from MRSA252)
    SACOL1960(gatB)aspartyl/glutamyl-tRNA amidotransferase subunit B  [5] (data from MRSA252)
    SACOL0460(guaB)inosine-5'-monophosphate dehydrogenase  [5] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [5] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [5] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [5] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [5] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [5] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [5] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [5] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [5] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [5] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [5] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [5] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [5] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [5] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [5] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [5] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [5] (data from MRSA252)
    SACOL1759universal stress protein  [5] (data from MRSA252)

Expression & Regulation[edit | edit source]

Operon[edit | edit source]

Regulation[edit | edit source]

  • regulator:

Transcription pattern[edit | edit source]

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

Protein stability[edit | edit source]

  • half-life: 208.27 h [6]

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, 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)
  3. 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)
  4. 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)
  5. 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 5.17 5.18 5.19 5.20 5.21 5.22 5.23 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)
  6. 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]