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NCBI: 26-AUG-2013

Summary[edit source | edit]

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

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SA0366 [new locus tag: SA_RS02095 ]
  • symbol: ahpC
  • product: alkyl hydroperoxide reductase
  • replicon: chromosome
  • strand: -
  • coordinates: 422549..423118
  • length: 570
  • essential: no DEG 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: SA0366 [new locus tag: SA_RS02095 ]
  • symbol: AhpC
  • description: alkyl hydroperoxide reductase
  • 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:  
    Thioredoxin-disulfide reductase Alkyl hydroperoxide reductase protein C (EC 1.11.1.15) 
  • PFAM:
    Thioredoxin (CL0172) AhpC-TSA; AhpC/TSA family (PF00578; HMM-score: 119.2)
    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:
    SA2428(arcA)arginine deiminase  [1] (data from MRSA252)
    SA1984(asp23)alkaline shock protein 23  [1] (data from MRSA252)
    SA1046(carB)carbamoyl phosphate synthase large subunit  [1] (data from MRSA252)
    SA1517(citC)isocitrate dehydrogenase  [1] (data from MRSA252)
    SA1409(dnaK)molecular chaperone DnaK  [1] (data from MRSA252)
    SA0731(eno)phosphopyruvate hydratase  [1] (data from MRSA252)
    SA0869(fabI)enoyl-ACP reductase  [1] (data from MRSA252)
    SA1029(ftsZ)cell division protein FtsZ  [1] (data from MRSA252)
    SA0505(fus)elongation factor G  [1] (data from MRSA252)
    SA1716(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [1] (data from MRSA252)
    SA1836(groEL)molecular chaperone GroEL  [1] (data from MRSA252)
    SA1305(hu)DNA-binding protein II  [1] (data from MRSA252)
    SA2400(mqo2)malate:quinone oxidoreductase  [1] (data from MRSA252)
    SA0943-1(pdhA)pyruvate dehydrogenase E1 component subunit alpha  [1] (data from MRSA252)
    SA1938(pdp)pyrimidine-nucleoside phosphorylase  [1] (data from MRSA252)
    SA0218(pflB)formate acetyltransferase  [1] (data from MRSA252)
    SA1520(pykA)pyruvate kinase  [1] (data from MRSA252)
    SA0496(rplA)50S ribosomal protein L1  [1] (data from MRSA252)
    SA2044(rplB)50S ribosomal protein L2  [1] (data from MRSA252)
    SA2047(rplC)50S ribosomal protein L3  [1] (data from MRSA252)
    SA2046(rplD)50S ribosomal protein L4  [1] (data from MRSA252)
    SA2033(rplF)50S ribosomal protein L6  [1] (data from MRSA252)
    SA0497(rplJ)50S ribosomal protein L10  [1] (data from MRSA252)
    SA0498(rplL)50S ribosomal protein L7/L12  [1] (data from MRSA252)
    SA2029(rplO)50S ribosomal protein L15  [1] (data from MRSA252)
    SA2040(rplP)50S ribosomal protein L16  [1] (data from MRSA252)
    SA2032(rplR)50S ribosomal protein L18  [1] (data from MRSA252)
    SA1084(rplS)50S ribosomal protein L19  [1] (data from MRSA252)
    SA1502(rplT)50S ribosomal protein L20  [1] (data from MRSA252)
    SA1473(rplU)50S ribosomal protein L21  [1] (data from MRSA252)
    SA2042(rplV)50S ribosomal protein L22  [1] (data from MRSA252)
    SA2045(rplW)50S ribosomal protein L23  [1] (data from MRSA252)
    SA2023(rpoA)DNA-directed RNA polymerase subunit alpha  [1] (data from MRSA252)
    SA1099(rpsB)30S ribosomal protein S2  [1] (data from MRSA252)
    SAS052(rpsD)30S ribosomal protein S4  [1] (data from MRSA252)
    SA2031(rpsE)30S ribosomal protein S5  [1] (data from MRSA252)
    SA2016(rpsI)30S ribosomal protein S9  [1] (data from MRSA252)
    SA2024(rpsK)30S ribosomal protein S11  [1] (data from MRSA252)
    SA2038(rpsQ)30S ribosomal protein S17  [1] (data from MRSA252)
    SA2043(rpsS)30S ribosomal protein S19  [1] (data from MRSA252)
    SA1245(sucA)2-oxoglutarate dehydrogenase E1  [1] (data from MRSA252)
    SA0506(tuf)elongation factor Tu  [1] (data from MRSA252)
    SA0627hypothetical protein  [1] (data from MRSA252)
    SA0802hypothetical protein  [1] (data from MRSA252)
    SA1532hypothetical protein  [1] (data from MRSA252)
    SA2327pyruvate 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
    • Ymax: 0.138
    • Ymax_pos: 16
    • Cmax: 0.129
    • Cmax_pos: 16
    • Smax: 0.26
    • Smax_pos: 15
    • Smean: 0.144
    • D: 0.14
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MSLINKEILPFTAQAFDPKKDQFKEVTQEDLKGSWSVVCFYPADFSFVCPTELEDLQNQYEELQKLGVNVFSVSTDTHFVHKAWHDHSDAISKITYTMIGDPSQTITRNFDVLDEATGLAQRGTFIIDPDGVVQASEINADGIGRDASTLAHKIKAAQYVRKNPGEVCPAKWEEGAKTLQPGLDLVGKI

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: SA1678 (PerR*)
    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: 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 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)

Relevant publications[edit source | edit]

Alexander Scherl, Patrice François, Manuela Bento, Jacques M Deshusses, Yvan Charbonnier, Véronique Converset, Antoine Huyghe, Nadia Walter, Christine Hoogland, Ron D Appel, Jean-Charles Sanchez, Catherine G Zimmermann-Ivol, Garry L Corthals, Denis F Hochstrasser, Jacques Schrenzel
Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth.
J. Microbiol. Methods: 2005, 60(2);247-57
[PubMed:15590099] [WorldCat.org] [DOI] (P p)