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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_02336
  • 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: SAOUHSC_02336
  • symbol: fabZ
  • product: (3R)-hydroxymyristoyl-ACP dehydratase
  • replicon: chromosome
  • strand: -
  • coordinates: 2164794..2165234
  • length: 441
  • essential: yes [1] DEG 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: SAOUHSC_02336
  • 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 [2] [3]
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • 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] [4]   other strains

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: no data available

⊟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. ↑ Roy R Chaudhuri, Andrew G Allen, Paul J Owen, Gil Shalom, Karl Stone, Marcus Harrison, Timothy A Burgis, Michael Lockyer, Jorge Garcia-Lara, Simon J Foster, Stephen J Pleasance, Sarah E Peters, Duncan J Maskell, Ian G Charles
    Comprehensive identification of essential Staphylococcus aureus genes using Transposon-Mediated Differential Hybridisation (TMDH).
    BMC Genomics: 2009, 10;291
    [PubMed:19570206] [WorldCat.org] [DOI] (I e)
  2. ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
    A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
    Proteomics: 2015, 15(21);3648-61
    [PubMed:26224020] [WorldCat.org] [DOI] (I p)
  3. ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
    A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
    Sci Rep: 2017, 7(1);9718
    [PubMed:28887440] [WorldCat.org] [DOI] (I e)
  4. ↑ 4.0 4.1 4.2 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
    Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
    PLoS Genet: 2016, 12(4);e1005962
    [PubMed:27035918] [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)

⊟Relevant publications[edit | edit source]

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