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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2091 [new locus tag: SACOL_RS10940 ]
  • pan locus tag?: SAUPAN005387000
  • symbol: fabZ
  • pan gene symbol?: fabZ
  • synonym:
  • product: (3R)-hydroxymyristoyl-ACP dehydratase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2091 [new locus tag: SACOL_RS10940 ]
  • symbol: fabZ
  • product: (3R)-hydroxymyristoyl-ACP dehydratase
  • replicon: chromosome
  • strand: -
  • coordinates: 2154070..2154510
  • length: 441
  • 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
    ATGGAAACAATTTTTGATTATAACCAAATTAAACAAATTATACCTCACAGACAGCCATTT
    TTATTAATTGATAAAGTAGTTGAATATGAAGAAGGTCAACGTTGTGTGGCTATTAAACAA
    GTATCAGGAAACGAACCATTCTTTCAAGGGCATTTTCCTGAGTATGCGGTAATGCCAGGC
    GTATTAATTACTGAAGCGTTAGCTCAAACAGGTGCGGTAGCTATTTTAAATAGTGAAGAA
    AATAAAGGTAAAATCGCTTTATTTGCTGGTATTGATAAATGTCGTTTTAAACGTCAAGTA
    GTACCTGGTGATACTTTAACGTTGGAAGTAGAAATCACTAAAATTAAAGGACCAATAGGT
    AAAGGTAATGCTAAAGCTACTGTCGATGGTCAACTTGCTTGTAGTTGTGAACTTACATTT
    GCAATTCAAGATGTAAAATAA
    60
    120
    180
    240
    300
    360
    420
    441

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2091 [new locus tag: SACOL_RS10940 ]
  • symbol: FabZ
  • description: (3R)-hydroxymyristoyl-ACP dehydratase
  • length: 146
  • theoretical pI: 5.78053
  • theoretical MW: 16081.5
  • GRAVY: -0.0369863

⊟Function[edit | edit source]

  • reaction:
    EC 4.2.1.59?  ExPASy
    3-hydroxyacyl-[acyl-carrier-protein] dehydratase A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O
  • TIGRFAM:
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabZ (TIGR01750; EC 4.2.1.-; HMM-score: 176.9)
    and 1 more
    Metabolism Fatty acid and phospholipid metabolism Biosynthesis beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA (TIGR01749; EC 4.2.1.59; HMM-score: 24.2)
  • TheSEED  :
    • 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, FabZ form (EC 4.2.1.59)
    Fatty Acids, Lipids, and Isoprenoids Fatty acids Fatty Acid Biosynthesis FASII  3-hydroxyacyl-[acyl-carrier-protein] dehydratase, FabZ form (EC 4.2.1.59)
  • PFAM:
    HotDog (CL0050) FabA; FabA-like domain (PF07977; HMM-score: 115.3)
    and 3 more
    MaoC_dehydratas; MaoC like domain (PF01575; HMM-score: 22)
    4HBT; Thioesterase superfamily (PF03061; HMM-score: 21.1)
    4HBT_2; Thioesterase-like superfamily (PF13279; HMM-score: 14.4)

⊟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): 0.002824
    • TAT(Tat/SPI): 0.000158
    • LIPO(Sec/SPII): 0.000279
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • METIFDYNQIKQIIPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEENKGKIALFAGIDKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAIQDVK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 390 [5]
  • 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;  [6] [7]   other strains

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 12.78 h [8]

⊟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. ↑ 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)
  7. ↑ 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)
  8. ↑ 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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