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NCBI: 03-AUG-2016

Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_01743
  • pan locus tag?: SAUPAN004240000
  • symbol: SAOUHSC_01743
  • pan gene symbol?: apt
  • synonym:
  • product: adenine phosphoribosyltransferase

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_01743
  • symbol: SAOUHSC_01743
  • product: adenine phosphoribosyltransferase
  • replicon: chromosome
  • strand: -
  • coordinates: 1646766..1647284
  • length: 519
  • essential: no 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
    421
    481
    ATGGATTTAAAGCAATACGTATCAGAAGTTCAAGATTGGCCGAAACCAGGTGTTAGTTTC
    AAGGATATTACTACAATTATGGATAATGGTGAAGCATATGGCTATGCAACAGATAAAATT
    GTAGAATACGCAAAAGACAGAGATGTTGATATCGTTGTAGGACCTGAAGCGCGTGGCTTT
    ATCATTGGCTGTCCTGTAGCTTATTCAATGGGGATTGGCTTTGCACCTGTTAGAAAAGAA
    GGGAAATTACCTCGTGAAGTCATTCGTTATGAGTATGACCTAGAATATGGTACAAATGTT
    TTAACAATGCACAAAGATGCAATTAAACCAGGTCAACGTGTGTTAATTACAGATGATTTA
    TTAGCTACTGGTGGTACGATTGAAGCAGCAATAAAATTAGTTGAAAAATTAGGCGGTATC
    GTAGTAGGTATTGCATTTATAATTGAATTGAAATATTTAAATGGTATTGAAAAAATTAAA
    GATTACGATGTTATGAGTTTAATCTCATACGACGAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    519

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: SAOUHSC_01743
  • symbol: SAOUHSC_01743
  • description: adenine phosphoribosyltransferase
  • length: 172
  • theoretical pI: 4.48452
  • theoretical MW: 19116.9
  • GRAVY: -0.030814

Function[edit | edit source]

  • reaction:
    EC 2.4.2.7?  ExPASy
    Adenine phosphoribosyltransferase AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate
  • TIGRFAM:
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides adenine phosphoribosyltransferase (TIGR01090; EC 2.4.2.7; HMM-score: 230.7)
    and 9 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis pur operon repressor PurR (TIGR01743; HMM-score: 47.6)
    Signal transduction Regulatory functions DNA interactions pur operon repressor PurR (TIGR01743; HMM-score: 47.6)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis orotate phosphoribosyltransferase (TIGR01367; EC 2.4.2.10; HMM-score: 44.1)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis orotate phosphoribosyltransferase (TIGR00336; EC 2.4.2.10; HMM-score: 37.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides xanthine phosphoribosyltransferase (TIGR01744; EC 2.4.2.22; HMM-score: 35.5)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis ribose-phosphate diphosphokinase (TIGR01251; EC 2.7.6.1; HMM-score: 27.9)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides uracil phosphoribosyltransferase (TIGR01091; EC 2.4.2.9; HMM-score: 19.3)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Salvage of nucleosides and nucleotides hypoxanthine phosphoribosyltransferase (TIGR01203; EC 2.4.2.8; HMM-score: 14.6)
    Cellular processes Cellular processes DNA transformation comF family protein (TIGR00201; HMM-score: 13.3)
  • TheSEED  :
    • Adenine phosphoribosyltransferase (EC 2.4.2.7)
    Nucleosides and Nucleotides Purines Purine conversions  Adenine phosphoribosyltransferase (EC 2.4.2.7)
    and 2 more
    Regulation and Cell signaling Regulation and Cell signaling - no subcategory cAMP signaling in bacteria  Adenine phosphoribosyltransferase (EC 2.4.2.7)
    Regulation and Cell signaling Regulation and Cell signaling - no subcategory Stringent Response, (p)ppGpp metabolism  Adenine phosphoribosyltransferase (EC 2.4.2.7)
  • PFAM:
    PRTase-like (CL0533) Pribosyltran; Phosphoribosyl transferase domain (PF00156; HMM-score: 53.7)
    and 1 more
    UPRTase; Uracil phosphoribosyltransferase (PF14681; HMM-score: 19.5)

Structure, modifications & cofactors[edit | edit source]

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

Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 10
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0
    • Extracellular Score: 0
    • 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): 0.018018
    • TAT(Tat/SPI): 0.000238
    • LIPO(Sec/SPII): 0.001122
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit | edit source]

Protein sequence[edit | edit source]

  • MDLKQYVSEVQDWPKPGVSFKDITTIMDNGEAYGYATDKIVEYAKDRDVDIVVGPEARGFIIGCPVAYSMGIGFAPVRKEGKLPREVIRYEYDLEYGTNVLTMHKDAIKPGQRVLITDDLLATGGTIEAAIKLVEKLGGIVVGIAFIIELKYLNGIEKIKDYDVMSLISYDE

Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas [1] [2]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SAOUHSC_01246(infB)translation initiation factor IF-2  [3] (data from MRSA252)
    SAOUHSC_00943(ppnK)inorganic polyphosphate/ATP-NAD kinase  [3] (data from MRSA252)
    SAOUHSC_01232(rpsB)30S ribosomal protein S2  [3] (data from MRSA252)
    SAOUHSC_00336acetyl-CoA acyltransferase  [3] (data from MRSA252)
    SAOUHSC_00679hypothetical protein  [3] (data from MRSA252)
    SAOUHSC_01416dihydrolipoamide succinyltransferase  [3] (data from MRSA252)

Expression & Regulation[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. 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)
  2. 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)
  3. 3.0 3.1 3.2 3.3 3.4 3.5 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)
  4. 4.0 4.1 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]