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NCBI: 06-JUL-2013

Summary[edit source | edit]

  • organism: Staphylococcus aureus Newman
  • locus tag: NWMN_1337 [new locus tag: NWMN_RS07535 ]
  • pan locus tag?: SAUPAN003858000
  • symbol: dfrA
  • pan gene symbol?: dfrA
  • synonym:
  • product: dihydrofolate reductase

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: NWMN_1337 [new locus tag: NWMN_RS07535 ]
  • symbol: dfrA
  • product: dihydrofolate reductase
  • replicon: chromosome
  • strand: -
  • coordinates: 1469966..1470445
  • length: 480
  • essential: unknown other strains

Accession numbers[edit source | edit]

Phenotype[edit source | edit]

  • Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 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 source | edit]

General[edit source | edit]

  • locus tag: NWMN_1337 [new locus tag: NWMN_RS07535 ]
  • symbol: DfrA
  • description: dihydrofolate reductase
  • length: 159
  • theoretical pI: 6.30297
  • theoretical MW: 18250.8
  • GRAVY: -0.210063

Function[edit source | edit]

  • reaction:
    EC 1.5.1.3?  ExPASy
    Dihydrofolate reductase5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH
  • TIGRFAM:
  • TheSEED:  
    Cofactors, Vitamins, Prosthetic Groups, PigmentsFolate and pterinesFolate Biosynthesis Dihydrofolate reductase (EC 1.5.1.3) 
  • PFAM:
    DHFred (CL0387) DHFR_1; Dihydrofolate reductase (PF00186; HMM-score: 184.4)
    SUKH (CL0526) SMI1_KNR4; SMI1 / KNR4 family (SUKH-1) (PF09346; HMM-score: 13.8)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:
    NWMN_2534(arcA)arginine deiminase  [1] (data from MRSA252)
    NWMN_1587(citC)isocitrate dehydrogenase  [1] (data from MRSA252)
    NWMN_1483(dnaK)molecular chaperone DnaK  [1] (data from MRSA252)
    NWMN_1096(ftsZ)cell division protein FtsZ  [1] (data from MRSA252)
    NWMN_0509(fus)elongation factor G  [1] (data from MRSA252)
    NWMN_0162(pflB)formate acetyltransferase  [1] (data from MRSA252)
    NWMN_0959(phdA)pyruvate dehydrogenase E1 component, alpha subunit  [1] (data from MRSA252)
    NWMN_1592(pykA)pyruvate kinase  [1] (data from MRSA252)
    NWMN_0500(rplA)50S ribosomal protein L1  [1] (data from MRSA252)
    NWMN_2149(rplB)50S ribosomal protein L2  [1] (data from MRSA252)
    NWMN_2152(rplC)50S ribosomal protein L3  [1] (data from MRSA252)
    NWMN_2140(rplE)50S ribosomal protein L5  [1] (data from MRSA252)
    NWMN_0502(rplL)50S ribosomal protein L7/L12  [1] (data from MRSA252)
    NWMN_2133(rplO)50S ribosomal protein L15  [1] (data from MRSA252)
    NWMN_1151(rplS)50S ribosomal protein L19  [1] (data from MRSA252)
    NWMN_1549(rplU)50S ribosomal protein L21  [1] (data from MRSA252)
    NWMN_2147(rplV)50S ribosomal protein L22  [1] (data from MRSA252)
    NWMN_2135(rpsE)30S ribosomal protein S5  [1] (data from MRSA252)
    NWMN_2119(rpsI)30S ribosomal protein S9  [1] (data from MRSA252)
    NWMN_2127(rpsK)30S ribosomal protein S11  [1] (data from MRSA252)
    NWMN_1325(sucB)dihydrolipoamide succinyltransferase  [1] (data from MRSA252)
    NWMN_0510(tufA)elongation factor Tu  [1] (data from MRSA252)
    NWMN_02495'-nucleotidase, lipoprotein e(P4) family protein  [1] (data from MRSA252)
    NWMN_0811hypothetical protein  [1] (data from MRSA252)
    NWMN_1382DNA-binding protein HU  [1] (data from MRSA252)
    NWMN_1604universal stress protein family protein  [1] (data from MRSA252)
    NWMN_1831ferritin  [1] (data from MRSA252)
    NWMN_2086alkaline shock protein 23  [1] (data from MRSA252)

Localization[edit source | edit]

  • 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
    • Ymax: 0.134
    • Ymax_pos: 17
    • Cmax: 0.115
    • Cmax_pos: 17
    • Smax: 0.212
    • Smax_pos: 13
    • Smean: 0.151
    • D: 0.141
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MTLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESIGKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEEMIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHTFLHLIRKK

Experimental data[edit source | edit]

  • experimentally validated: no data available

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: no data available

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  1. 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 1.27 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)

Relevant publications[edit source | edit]