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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2104 [new locus tag: SACOL_RS11010 ]
  • pan locus tag?: SAUPAN005403000
  • symbol: upp
  • pan gene symbol?: upp
  • synonym:
  • product: uracil phosphoribosyltransferase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2104 [new locus tag: SACOL_RS11010 ]
  • symbol: upp
  • product: uracil phosphoribosyltransferase
  • replicon: chromosome
  • strand: -
  • coordinates: 2164933..2165562
  • length: 630
  • 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
    ATGAGTAAAGTACACGTTTTCGATCATCCATTAATTCAACACAAACTAAGCTATATTAGA
    GATGTAAATACAGGTACTAAAGAATTTAGAGAACTTGTAGACGAAGTTGGTATGTTGATG
    GCATATGAAGTAACTAGAGACTTAGAGCTTCAGGATGTTGATATTGAAACGCCTGTAACT
    AAAATGACGGCTAAACGATTAGCTGGTAAAAAATTAGCTATCGTTCCAATTTTAAGAGCT
    GGTTTAGGTATGACTGATGGTATTTTAAGTTTAGTACCTGCAGCCAGAGTTGGACATATC
    GGTTTATATCGAGATCCCGAAACATTAAAGGCTGTAGAGTATTTTGCTAAGTTACCTCAA
    GATATTACTGAAAGACAAATCATTGTTGTTGATCCTATGTTAGCAACAGGCGCATCAGCA
    ATTGAAGCTATTACTTCATTGAAGAAACGTGGCGCTAAAAATATTCGCTTCATGTGTTTA
    ATTGCAGCACCAGAAGGCGTAGAAAAGATGCATGAAGCACATCCAGATGTAGATATTTAT
    ATTGCTGCACTTGATGAAAAGCTAAATGACAAAGCATATATCACACCAGGGTTAGGCGAC
    GCTGGAGATAGATTGTTTGGTACTAAATAG
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    630

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2104 [new locus tag: SACOL_RS11010 ]
  • symbol: Upp
  • description: uracil phosphoribosyltransferase
  • length: 209
  • theoretical pI: 6.52063
  • theoretical MW: 23049.7
  • GRAVY: -0.0320574

⊟Function[edit | edit source]

  • reaction:
    EC 2.4.2.9?  ExPASy
    Uracil phosphoribosyltransferase UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
  • TIGRFAM:
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides uracil phosphoribosyltransferase (TIGR01091; EC 2.4.2.9; HMM-score: 304.6)
    and 6 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis ribose-phosphate diphosphokinase (TIGR01251; EC 2.7.6.1; HMM-score: 27.5)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis orotate phosphoribosyltransferase (TIGR01367; EC 2.4.2.10; HMM-score: 23)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides hypoxanthine phosphoribosyltransferase (TIGR01203; EC 2.4.2.8; HMM-score: 22.8)
    Cellular processes Cellular processes DNA transformation comF family protein (TIGR00201; HMM-score: 17.1)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides adenine phosphoribosyltransferase (TIGR01090; EC 2.4.2.7; HMM-score: 12.9)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis orotate phosphoribosyltransferase (TIGR00336; EC 2.4.2.10; HMM-score: 12.1)
  • TheSEED  :
    • Uracil phosphoribosyltransferase (EC 2.4.2.9)
    Nucleosides and Nucleotides Pyrimidines De Novo Pyrimidine Synthesis  Uracil phosphoribosyltransferase (EC 2.4.2.9)
    and 1 more
    Nucleosides and Nucleotides Pyrimidines pyrimidine conversions  Uracil phosphoribosyltransferase (EC 2.4.2.9)
  • PFAM:
    PRTase-like (CL0533) UPRTase; Uracil phosphoribosyltransferase (PF14681; HMM-score: 258.9)
    and 1 more
    Pribosyltran; Phosphoribosyl transferase domain (PF00156; HMM-score: 42.2)

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

  • domains:
  • modifications:
  • cofactors: Mg2+
  • 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): 0.002006
    • TAT(Tat/SPI): 0.000137
    • LIPO(Sec/SPII): 0.000193
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSKVHVFDHPLIQHKLSYIRDVNTGTKEFRELVDEVGMLMAYEVTRDLELQDVDIETPVTKMTAKRLAGKKLAIVPILRAGLGMTDGILSLVPAARVGHIGLYRDPETLKAVEYFAKLPQDITERQIIVVDPMLATGASAIEAITSLKKRGAKNIRFMCLIAAPEGVEKMHEAHPDVDIYIAALDEKLNDKAYITPGLGDAGDRLFGTK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 2112 [5]
  • interaction partners:
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL25691-pyrroline-5-carboxylate dehydrogenase  [6] (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: 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. ↑ 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. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 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)

⊟Relevant publications[edit | edit source]

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