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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2321 [new locus tag: SACOL_RS12205 ]
  • pan locus tag?: SAUPAN005813000
  • symbol: SACOL2321
  • pan gene symbol?: —
  • synonym:
  • product: short chain dehydrogenase/reductase oxidoreductase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2321 [new locus tag: SACOL_RS12205 ]
  • symbol: SACOL2321
  • product: short chain dehydrogenase/reductase oxidoreductase
  • replicon: chromosome
  • strand: -
  • coordinates: 2382111..2382992
  • length: 882
  • 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
    601
    661
    721
    781
    841
    ATGGCAGCTCAAGATCCTAGAACAAAATTTAAAACAACGGATTATGAAAAACAAGAACAA
    GAGGTACCGGGTTTACAATCTGAAATGACGCCAGCACCCGATTGTGGCGAAACGTCTTAC
    CAAGGTCATCAACGCTTACAAGGCTATAAAATATTAGTCACAGGTGGTGACTCAGCAATA
    GGGCGTGCAGCAGCAATTGCGTATGCTAAAGAAGGTGCAGATGTAGCGATTAACTATCTT
    CCGAGTGAAGAACAAGATGCACAAGAAGTACGCCAAGTGATTGAAGAAAGTGGTCAAAAG
    GCAGTGTTAATTCCTGGTGATATAAGAGATGAACAGTTCAACTATGACCTTGTTGAACAA
    GCATATCAACAATTAGGTGGCTTAGATAATGTTACTTTAGTTGCTGGACATCAACAGTAT
    CATGATGATATTCATGGATTTACAACTGAGGCATTTACAGAAACATTTGAAACGAATGTC
    TATCCGCTATTTTGGACAGTTCAAAAAGCATTGGAATATTTAAAACCGGGTGCGTCAATT
    ACAACGACATCATCTGTACAAGGTTATAATCCTAGTCCTATTCTTCATGATTATGCCGCT
    TCAAAAGCAGCAATTATTTCATTAACTAAAAGTTTTTCAGAAGAATTAGGACCAAAAGGA
    ATTAGAGTGAACTGTGTAGCGCCTGGTCCATTCTGGTCACCATTACAAATTTCTGGTGGA
    CAACCTCAAAGTAAAATCCCAACATTTGGTCAAAAAACACCTTTAGGTCGTGCAGGTCAA
    CCTGTTGAGTTATGTGGAACTTATGTGCTATTAGCGTCAGAAGAATCAAGTTATACAACC
    GGACAAGTGTTCGGTGTTAGCGGTGGAGTGCAAATAGATTAG
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    882

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2321 [new locus tag: SACOL_RS12205 ]
  • symbol: SACOL2321
  • description: short chain dehydrogenase/reductase oxidoreductase
  • length: 293
  • theoretical pI: 4.3889
  • theoretical MW: 31734
  • GRAVY: -0.395563

⊟Function[edit | edit source]

  • TIGRFAM:
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase (TIGR01830; EC 1.1.1.100; HMM-score: 139.7)
    Unknown function Enzymes of unknown specificity SDR family mycofactocin-dependent oxidoreductase (TIGR03971; EC 1.1.99.-; HMM-score: 127.1)
    Metabolism Energy metabolism Fermentation acetoin reductases (TIGR02415; EC 1.1.1.-; HMM-score: 117.9)
    and 10 more
    Metabolism Energy metabolism Biosynthesis and degradation of polysaccharides 2-deoxy-D-gluconate 3-dehydrogenase (TIGR01832; EC 1.1.1.125; HMM-score: 104.6)
    2-hydroxycyclohexanecarboxyl-CoA dehydrogenase (TIGR03206; EC 1.1.1.-; HMM-score: 94.5)
    3-hydroxybutyrate dehydrogenase (TIGR01963; HMM-score: 92.4)
    acetoacetyl-CoA reductase (TIGR01829; EC 1.1.1.36; HMM-score: 90.5)
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis putative 3-oxoacyl-(acyl-carrier-protein) reductase (TIGR01831; HMM-score: 90.1)
    cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (TIGR03325; EC 1.3.1.56; HMM-score: 82.5)
    2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (TIGR04316; EC 1.3.1.28; HMM-score: 77.8)
    rhamnulose-1-phosphate aldolase/alcohol dehydrogenase (TIGR02632; EC 1.1.1.1,4.1.2.19; HMM-score: 72.6)
    Unknown function Enzymes of unknown specificity SDR family mycofactocin-dependent oxidoreductase (TIGR04504; EC 1.1.99.-; HMM-score: 62.5)
    pteridine reductase (TIGR02685; EC 1.5.1.33; HMM-score: 56.6)
  • TheSEED  :
    • Putative oxidoreductase
  • PFAM:
    NADP_Rossmann (CL0063) adh_short_C2; Enoyl-(Acyl carrier protein) reductase (PF13561; HMM-score: 177.7)
    and 4 more
    adh_short; short chain dehydrogenase (PF00106; HMM-score: 142)
    KR; KR domain (PF08659; HMM-score: 33.2)
    Epimerase; NAD dependent epimerase/dehydratase family (PF01370; HMM-score: 19.6)
    GDP_Man_Dehyd; GDP-mannose 4,6 dehydratase (PF16363; HMM-score: 11.5)

⊟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: -1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.072169
    • TAT(Tat/SPI): 0.003634
    • LIPO(Sec/SPII): 0.002331
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MAAQDPRTKFKTTDYEKQEQEVPGLQSEMTPAPDCGETSYQGHQRLQGYKILVTGGDSAIGRAAAIAYAKEGADVAINYLPSEEQDAQEVRQVIEESGQKAVLIPGDIRDEQFNYDLVEQAYQQLGGLDNVTLVAGHQQYHDDIHGFTTEAFTETFETNVYPLFWTVQKALEYLKPGASITTTSSVQGYNPSPILHDYAASKAAIISLTKSFSEELGPKGIRVNCVAPGPFWSPLQISGGQPQSKIPTFGQKTPLGRAGQPVELCGTYVLLASEESSYTTGQVFGVSGGVQID

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 1857 [4]
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: SigB* (activation) regulon
    SigB*(sigma factor)controlling a large regulon involved in stress/starvation response and adaptation;  [5] [6]   other strains

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 29.12 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, 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)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ Markus Bischoff, Paul Dunman, Jan Kormanec, Daphne Macapagal, Ellen Murphy, William Mounts, Brigitte Berger-Bächi, Steven Projan
    Microarray-based analysis of the Staphylococcus aureus sigmaB regulon.
    J Bacteriol: 2004, 186(13);4085-99
    [PubMed:15205410] [WorldCat.org] [DOI] (P p)
  6. ↑ Jan Pané-Farré, Beate Jonas, Konrad Förstner, Susanne Engelmann, Michael Hecker
    The sigmaB regulon in Staphylococcus aureus and its regulation.
    Int J Med Microbiol: 2006, 296(4-5);237-58
    [PubMed:16644280] [WorldCat.org] [DOI] (P 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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