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NCBI: 02-MAR-2017

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA_RS02095 [old locus tag: SA0366 ]
  • pan locus tag?: SAUPAN001982000
  • symbol: SA_RS02095
  • pan gene symbol?: ahpC
  • synonym:
  • product: alkyl hydroperoxide reductase subunit C

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SA_RS02095 [old locus tag: SA0366 ]
  • symbol: SA_RS02095
  • product: alkyl hydroperoxide reductase subunit C
  • replicon: chromosome
  • strand: -
  • coordinates: 422549..423118
  • length: 570
  • essential: no DEG other strains

⊟Accession numbers[edit | edit source]

  • Location: NC_002745 (422549..423118) NCBI
  • BioCyc: SA_RS02095 BioCyc
  • MicrobesOnline: see SA0366

⊟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
    ATGTCATTAATTAACAAAGAAATCTTACCATTTACAGCGCAAGCTTTCGATCCAAAAAAA
    GATCAATTTAAAGAAGTTACACAAGAAGATTTAAAAGGTTCTTGGAGCGTAGTATGCTTC
    TATCCTGCTGACTTCTCATTCGTTTGTCCAACTGAATTAGAAGACTTACAAAACCAATAT
    GAAGAATTACAAAAATTAGGCGTAAATGTATTCTCAGTATCAACTGATACTCACTTCGTA
    CACAAAGCATGGCATGACCATTCAGATGCAATTAGCAAAATCACTTACACTATGATTGGT
    GACCCATCACAAACAATCACTCGTAATTTTGATGTATTAGATGAAGCTACTGGTTTAGCT
    CAACGTGGTACATTCATTATCGACCCAGACGGTGTTGTACAAGCATCTGAAATTAACGCT
    GACGGAATTGGCCGTGACGCTAGTACATTAGCTCACAAAATCAAAGCAGCTCAATATGTT
    CGTAAAAACCCTGGCGAAGTATGCCCAGCTAAATGGGAAGAAGGCGCTAAAACATTGCAA
    CCTGGTTTAGATTTAGTAGGTAAAATCTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    570

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SA_RS02095 [old locus tag: SA0366 ]
  • symbol: SA_RS02095
  • description: alkyl hydroperoxide reductase subunit C
  • length: 189
  • theoretical pI: 4.6567
  • theoretical MW: 20976.5
  • GRAVY: -0.331217

⊟Function[edit | edit source]

  • reaction:
    EC 1.11.1.15?  ExPASy
    Peroxiredoxin 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
  • TIGRFAM:
    Cellular processes Cellular processes Detoxification peroxiredoxin (TIGR03137; EC 1.11.1.15; HMM-score: 321.6)
    Cellular processes Cellular processes Adaptations to atypical conditions peroxiredoxin (TIGR03137; EC 1.11.1.15; HMM-score: 321.6)
  • TheSEED: see SA0366
  • PFAM:
    Thioredoxin (CL0172) AhpC-TSA; AhpC/TSA family (PF00578; HMM-score: 119.2)
    and 4 more
    Redoxin; Redoxin (PF08534; HMM-score: 52.2)
    no clan defined 1-cysPrx_C; C-terminal domain of 1-Cys peroxiredoxin (PF10417; HMM-score: 25)
    Thioredoxin (CL0172) SCO1-SenC; SCO1/SenC (PF02630; HMM-score: 21.2)
    Glyco_hydro_tim (CL0058) NAGidase; beta-N-acetylglucosaminidase (PF07555; HMM-score: 12.6)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • Internal Helices: 0
  • LocateP:
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.012719
    • TAT(Tat/SPI): 0.000229
    • LIPO(Sec/SPII): 0.000739
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSLINKEILPFTAQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYVRKNPGEVCPAKWEEGAKTLQPGLDLVGKI

⊟Experimental data[edit | edit source]

  • experimentally validated: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SA_RS11130(deoA)pyrimidine-nucleoside phosphorylase  [1] (data from MRSA252)
    SA_RS09855(gatA)glutamyl-tRNA(Gln) amidotransferase subunit A  [1] (data from MRSA252)
    SA_RS01275formate acetyltransferase  [1] (data from MRSA252)
    SA_RS0291050S ribosomal protein L1  [1] (data from MRSA252)
    SA_RS0291550S ribosomal protein L10  [1] (data from MRSA252)
    SA_RS0292050S ribosomal protein L7/L12  [1] (data from MRSA252)
    SA_RS02955elongation factor G  [1] (data from MRSA252)
    SA_RS02960elongation factor Tu  [1] (data from MRSA252)
    SA_RS04160enolase  [1] (data from MRSA252)
    SA_RS04575NADH dehydrogenase  [1] (data from MRSA252)
    SA_RS04915enoyl-ACP reductase  [1] (data from MRSA252)
    SA_RS05350pyruvate dehydrogenase E1 component subunit alpha  [1] (data from MRSA252)
    SA_RS05860cell division protein FtsZ  [1] (data from MRSA252)
    SA_RS05945carbamoyl-phosphate synthase large chain  [1] (data from MRSA252)
    SA_RS0614050S ribosomal protein L19  [1] (data from MRSA252)
    SA_RS0622530S ribosomal protein S2  [1] (data from MRSA252)
    SA_RS070652-oxoglutarate dehydrogenase E1 component  [1] (data from MRSA252)
    SA_RS07385DNA-binding protein HU  [1] (data from MRSA252)
    SA_RS07955molecular chaperone DnaK  [1] (data from MRSA252)
    SA_RS0829550S ribosomal protein L21  [1] (data from MRSA252)
    SA_RS0846050S ribosomal protein L20  [1] (data from MRSA252)
    SA_RS08545isocitrate dehydrogenase (NADP(+))  [1] (data from MRSA252)
    SA_RS08560pyruvate kinase  [1] (data from MRSA252)
    SA_RS08625universal stress protein UspA  [1] (data from MRSA252)
    SA_RS0867530S ribosomal protein S4  [1] (data from MRSA252)
    SA_RS10535molecular chaperone GroEL  [1] (data from MRSA252)
    SA_RS11430Asp23/Gls24 family envelope stress response protein  [1] (data from MRSA252)
    SA_RS1160030S ribosomal protein S9  [1] (data from MRSA252)
    SA_RS11635DNA-directed RNA polymerase subunit alpha  [1] (data from MRSA252)
    SA_RS1164030S ribosomal protein S11  [1] (data from MRSA252)
    SA_RS1167050S ribosomal protein L15  [1] (data from MRSA252)
    SA_RS1168030S ribosomal protein S5  [1] (data from MRSA252)
    SA_RS1168550S ribosomal protein L18  [1] (data from MRSA252)
    SA_RS1169050S ribosomal protein L6  [1] (data from MRSA252)
    SA_RS1172030S ribosomal protein S17  [1] (data from MRSA252)
    SA_RS1173050S ribosomal protein L16  [1] (data from MRSA252)
    SA_RS1174050S ribosomal protein L22  [1] (data from MRSA252)
    SA_RS1174530S ribosomal protein S19  [1] (data from MRSA252)
    SA_RS1175050S ribosomal protein L2  [1] (data from MRSA252)
    SA_RS1175550S ribosomal protein L23  [1] (data from MRSA252)
    SA_RS1176050S ribosomal protein L4  [1] (data from MRSA252)
    SA_RS1176550S ribosomal protein L3  [1] (data from MRSA252)
    SA_RS13340pyruvate oxidase  [1] (data from MRSA252)
    SA_RS13735malate:quinone oxidoreductase  [1] (data from MRSA252)
    SA_RS13920arginine deiminase  [1] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

⊟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. ↑ 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 1.28 1.29 1.30 1.31 1.32 1.33 1.34 1.35 1.36 1.37 1.38 1.39 1.40 1.41 1.42 1.43 1.44 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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