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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2173 [new locus tag: SACOL_RS11435 ]
  • pan locus tag?: SAUPAN005578000
  • symbol: SACOL2173
  • pan gene symbol?: asp23
  • synonym:
  • product: alkaline shock protein 23

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2173 [new locus tag: SACOL_RS11435 ]
  • symbol: SACOL2173
  • product: alkaline shock protein 23
  • replicon: chromosome
  • strand: -
  • coordinates: 2255446..2255955
  • length: 510
  • 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
    ATGACTGTAGATAACAATAAAGCAAAACAAGCATACGACAATCAAACTGGTGTTAACGAA
    AAAGAAAGAGAAGAGCGTCAAAAACAACAAGAACAAAATCAGGAGCCTCAATTCAAAAAC
    AAATTAACATTCTCTGATGAAGTTGTTGAAAAAATTGCTGGTATCGCTGCACGTGAAGTT
    AAAGGTATCTTAGATATGAAAGGTGGCTTAACTGATACATTCACTAATGCATTCTCAAGT
    GGCAACAATGTTACTCAAGGTGTATCTGTTGAAGTTGGTGAAAAACAAGCTGCTGTAGAC
    TTAAAAGTAATCTTAGAATATGGTGAATCAGCACCAAAAATCTTCCGTAAAGTAACTGAA
    TTAGTTAAAGAACAAGTTAAATATATTACTGGTTTAGATGTAGTTGAAGTTAACATGCAA
    GTTGACGATGTAATGACTCAAAAAGAGTGGAAACAAAAACACGAAAAAAATAACGAAAAC
    AATAACCAAGAAAGACAAGGTTTACAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    510

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2173 [new locus tag: SACOL_RS11435 ]
  • symbol: SACOL2173
  • description: alkaline shock protein 23
  • length: 169
  • theoretical pI: 4.8448
  • theoretical MW: 19191.3
  • GRAVY: -0.956805

⊟Function[edit | edit source]

  • TIGRFAM:
  • TheSEED  :
    • Alkaline shock protein 23
  • PFAM:
    no clan defined Asp23; Asp23 family, cell envelope-related function (PF03780; HMM-score: 117)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: unknown (no significant prediction)
    • Cytoplasmic Score: 2.5
    • Cytoplasmic Membrane Score: 2.5
    • Cellwall Score: 2.5
    • Extracellular Score: 2.5
    • 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): 0.007466
    • TAT(Tat/SPI): 0.00095
    • LIPO(Sec/SPII): 0.001397
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTVDNNKAKQAYDNQTGVNEKEREERQKQQEQNQEPQFKNKLTFSDEVVEKIAGIAAREVKGILDMKGGLTDTFTNAFSSGNNVTQGVSVEVGEKQAAVDLKVILEYGESAPKIFRKVTELVKEQVKYITGLDVVEVNMQVDDVMTQKEWKQKHEKNNENNNQERQGLQ

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4] [5]
  • quantitative data / protein copy number per cell: 13781 [6]
  • interaction partners:
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [7] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [7] (data from MRSA252)
    SACOL2239(rplC)50S ribosomal protein L3  [7] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [7] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [7] (data from MRSA252)
    SACOL0211acetyl-CoA acetyltransferase  [7] (data from MRSA252)
    SACOL02123-hydroxyacyl-CoA dehydrogenase  [7] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [7] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [7] (data from MRSA252)

⊟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 [8] [9]   other strains

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 27.76 h [10]

⊟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. ↑ Annette Dreisbach, Kristina Hempel, Girbe Buist, Michael Hecker, Dörte Becher, Jan Maarten van Dijl
    Profiling the surfacome of Staphylococcus aureus.
    Proteomics: 2010, 10(17);3082-96
    [PubMed:20662103] [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. ↑ 7.0 7.1 7.2 7.3 7.4 7.5 7.6 7.7 7.8 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)
  8. ↑ 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)
  9. ↑ 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)
  10. ↑ 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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