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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0452 [new locus tag: SACOL_RS02285 ]
  • pan locus tag?: SAUPAN001982000
  • symbol: ahpC
  • 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: SACOL0452 [new locus tag: SACOL_RS02285 ]
  • symbol: ahpC
  • product: alkyl hydroperoxide reductase subunit C
  • replicon: chromosome
  • strand: -
  • coordinates: 453332..453901
  • length: 570
  • 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
    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: SACOL0452 [new locus tag: SACOL_RS02285 ]
  • symbol: AhpC
  • 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]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 12844 [5]
  • interaction partners:
    SACOL2657(arcA)arginine deiminase  [6] (data from MRSA252)
    SACOL1215(carB)carbamoyl phosphate synthase large subunit  [6] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [6] (data from MRSA252)
    SACOL1016(fabI)enoyl-ACP reductase  [6] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL1961(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [6] (data from MRSA252)
    SACOL2016(groEL)chaperonin GroEL  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [6] (data from MRSA252)
    SACOL2238(rplD)50S ribosomal protein L4  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL2232(rplP)50S ribosomal protein L16  [6] (data from MRSA252)
    SACOL2223(rplR)50S ribosomal protein L18  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [6] (data from MRSA252)
    SACOL2213(rpoA)DNA-directed RNA polymerase subunit alpha  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [6] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [6] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)
    SACOL2553pyruvate oxidase  [6] (data from MRSA252)

⊟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: 17.58 h [7]

⊟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. ↑ Kristina Hempel, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J Proteome Res: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  3. ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
    Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
    J Proteome Res: 2011, 10(4);1657-66
    [PubMed:21323324] [WorldCat.org] [DOI] (I p)
  4. ↑ 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)
  5. ↑ 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)
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 6.32 6.33 6.34 6.35 6.36 6.37 6.38 6.39 6.40 6.41 6.42 6.43 6.44 6.45 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)
  7. ↑ 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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