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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_00365
  • pan locus tag?: SAUPAN001982000
  • symbol: SAOUHSC_00365
  • 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: SAOUHSC_00365
  • symbol: SAOUHSC_00365
  • product: alkyl hydroperoxide reductase subunit C
  • replicon: chromosome
  • strand: -
  • coordinates: 371268..371837
  • length: 570
  • 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
    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: SAOUHSC_00365
  • symbol: SAOUHSC_00365
  • 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  :
    • NADH-dependent alkyl hydroperoxide reductase component AhpC (EC 1.11.1.26)
    Sulfur Metabolism Sulfur Metabolism - no subcategory Thioredoxin-disulfide reductase  Alkyl hydroperoxide reductase protein C (EC 1.6.4.-)
  • 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: Intracellular
    • Prediction by SwissProt Classification: Cytoplasmic
    • Pathway Prediction: No pathway
    • Intracellular possibility: 1
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: 0
    • Predicted Cleavage Site: No CleavageSite
  • 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]

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: PerR* (repression) regulon
    PerR*(TF)important in Oxidative stress response; RegPrecise 

⊟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. ↑ 3.00 3.01 3.02 3.03 3.04 3.05 3.06 3.07 3.08 3.09 3.10 3.11 3.12 3.13 3.14 3.15 3.16 3.17 3.18 3.19 3.20 3.21 3.22 3.23 3.24 3.25 3.26 3.27 3.28 3.29 3.30 3.31 3.32 3.33 3.34 3.35 3.36 3.37 3.38 3.39 3.40 3.41 3.42 3.43 3.44 3.45 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]

Julie A Morrissey, Alan Cockayne, Kirsty Brummell, Paul Williams
The staphylococcal ferritins are differentially regulated in response to iron and manganese and via PerR and Fur.
Infect Immun: 2004, 72(2);972-9
[PubMed:14742543] [WorldCat.org] [DOI] (P p)Kate Cosgrove, Graham Coutts, Ing-Marie Jonsson, Andrej Tarkowski, John F Kokai-Kun, James J Mond, Simon J Foster
Catalase (KatA) and alkyl hydroperoxide reductase (AhpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence, and nasal colonization in Staphylococcus aureus.
J Bacteriol: 2007, 189(3);1025-35
[PubMed:17114262] [WorldCat.org] [DOI] (P p)L Armstrong-Buisseret, M B Cole, G S Stewart
A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is induced by osmotic upshock in Staphylococcus aureus.
Microbiology (Reading): 1995, 141 ( Pt 7);1655-61
[PubMed:7551034] [WorldCat.org] [DOI] (P p)

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