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NCBI: 10-JUN-2013

⊟Summary[edit source | edit]

  • 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 source | edit]

⊟Gene[edit source | edit]

⊟General[edit source | edit]

  • 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 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
    481
    541
    ATGTCATTAATTAACAAAGAAATCTTACCATTTACAGCGCAAGCTTTCGATCCAAAAAAA
    GATCAATTTAAAGAAGTTACACAAGAAGATTTAAAAGGTTCTTGGAGCGTAGTATGCTTC
    TATCCTGCTGACTTCTCATTCGTTTGTCCAACTGAATTAGAAGACTTACAAAACCAATAT
    GAAGAATTACAAAAATTAGGCGTAAATGTATTCTCAGTATCAACTGATACTCACTTCGTA
    CACAAAGCATGGCATGACCATTCAGATGCAATTAGCAAAATCACTTACACTATGATTGGT
    GACCCATCACAAACAATCACTCGTAATTTTGATGTATTAGATGAAGCTACTGGTTTAGCT
    CAACGTGGTACATTCATTATCGACCCAGACGGTGTTGTACAAGCATCTGAAATTAACGCT
    GACGGAATTGGCCGTGACGCTAGTACATTAGCTCACAAAATCAAAGCAGCTCAATATGTT
    CGTAAAAACCCTGGCGAAGTATGCCCAGCTAAATGGGAAGAAGGCGCTAAAACATTGCAA
    CCTGGTTTAGATTTAGTAGGTAAAATCTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    570

⊟Protein[edit source | edit]

⊟General[edit source | edit]

  • 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 source | edit]

  • reaction:
    EC 1.11.1.15?  ExPASy
    Peroxiredoxin2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
  • TIGRFAM:
    Cellular processesCellular processesDetoxificationperoxiredoxin (TIGR03137; EC 1.11.1.15; HMM-score: 321.6)
    Cellular processesCellular processesAdaptations to atypical conditionsperoxiredoxin (TIGR03137; EC 1.11.1.15; HMM-score: 321.6)
  • TheSEED:  
    Sulfur MetabolismSulfur Metabolism - no subcategoryThioredoxin-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 defined1-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 & interactions[edit source | edit]

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

⊟Localization[edit source | edit]

  • 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 source | edit]

⊟Protein sequence[edit source | edit]

  • MSLINKEILPFTAQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYVRKNPGEVCPAKWEEGAKTLQPGLDLVGKI

⊟Experimental data[edit source | edit]

  • experimentally validated: PeptideAtlas
    experimental localization: Cytoplasmic [2] [3] [4] [5]
    quantitative data / protein copy number per cell: 12844 [6]

⊟Expression & Regulation[edit source | edit]

⊟Operon[edit source | edit]

⊟Regulation[edit source | edit]

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

⊟Transcription pattern[edit source | edit]

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

⊟Protein stability[edit source | edit]

  • half-life: 17.58 h [7]

⊟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 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 1.45 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)
  2. ↑ 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)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ 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)
  6. ↑ 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)
  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 source | edit]

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