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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1461 [new locus tag: SACOL_RS07460 ]
  • pan locus tag?: SAUPAN003858000
  • symbol: folA
  • pan gene symbol?: dfrA
  • synonym:
  • product: dihydrofolate reductase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1461 [new locus tag: SACOL_RS07460 ]
  • symbol: folA
  • product: dihydrofolate reductase
  • replicon: chromosome
  • strand: -
  • coordinates: 1473786..1474265
  • 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
    ATGACTTTATCCATTCTAGTTGCACATGACTTGCAACGAGTAATTGGTTTTGAAAATCAA
    TTACCTTGGCACCTACCAAATGATTTGAAGCATGTTAAAAAATTATCAACAGGTCATACT
    TTAGTAATGGGTCGTAAGACATTTGAATCGATTGGTAAACCACTACCGAATCGTCGAAAT
    GTTGTACTTACTTCAGATACAAGTTTCAACGTAGAGGGCGTTGATGTAATTCACTCTATT
    GAAGATATTTACCAACTACCGGGCCATGTTTTCATATTTGGAGGGCAAACATTATTTGAA
    GAAATGATTGATAAAGTGGACGACATGTATATTACTGTTATTGAAGGTAAATTCCGTGGT
    GATACGTTCTTTCCACCTTATACATTTGAAGACTGGGAAGTTGCCTCTTCAGTTGAAGGT
    AAACTAGATGAGAAAAATACAATTCCACATACCTTTCTACATTTAATTCGTAAAAAATAA
    60
    120
    180
    240
    300
    360
    420
    480

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1461 [new locus tag: SACOL_RS07460 ]
  • symbol: FolA
  • description: dihydrofolate reductase
  • length: 159
  • theoretical pI: 6.30297
  • theoretical MW: 18250.8
  • GRAVY: -0.210063

⊟Function[edit | edit source]

  • reaction:
    EC 1.5.1.3?  ExPASy
    Dihydrofolate reductase 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH
  • TIGRFAM:
  • TheSEED  :
    • Dihydrofolate reductase (EC 1.5.1.3)
    Cofactors, Vitamins, Prosthetic Groups, Pigments Folate and pterines Folate Biosynthesis  Dihydrofolate reductase (EC 1.5.1.3)
  • PFAM:
    DHFred (CL0387) DHFR_1; Dihydrofolate reductase (PF00186; HMM-score: 184.4)
    and 1 more
    SUKH (CL0526) SMI1_KNR4; SMI1 / KNR4 family (SUKH-1) (PF09346; HMM-score: 13.8)

⊟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): 0.003424
    • TAT(Tat/SPI): 0.000394
    • LIPO(Sec/SPII): 0.00044
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2]
  • quantitative data / protein copy number per cell: 181 [3]
  • interaction partners:
    SACOL2657(arcA)arginine deiminase  [4] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [4] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [4] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [4] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [4] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [4] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [4] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [4] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [4] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [4] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [4] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [4] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [4] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [4] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [4] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [4] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [4] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [4] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [4] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [4] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [4] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [4] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [4] (data from MRSA252)
    SACOL03035'-nucleotidase  [4] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [4] (data from MRSA252)
    SACOL1759universal stress protein  [4] (data from MRSA252)
    SACOL1952ferritins family protein  [4] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [4] (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: 42.52 h [5]

⊟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. ↑ 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)
  3. ↑ 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)
  4. ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 4.19 4.20 4.21 4.22 4.23 4.24 4.25 4.26 4.27 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)
  5. ↑ 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]

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