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NCBI: 03-AUG-2016

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus NCTC8325
  • locus tag: SAOUHSC_00985
  • pan locus tag?: SAUPAN003248000
  • symbol: SAOUHSC_00985
  • pan gene symbol?: menB
  • synonym:
  • product: 1,4-dihydroxy-2-naphthoyl-CoA synthase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SAOUHSC_00985
  • symbol: SAOUHSC_00985
  • product: 1,4-dihydroxy-2-naphthoyl-CoA synthase
  • replicon: chromosome
  • strand: +
  • coordinates: 956726..957547
  • length: 822
  • essential: no [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
    481
    541
    601
    661
    721
    781
    ATGACTAACAGACAATGGGAAACACTTAGAGAATATGATGAAATCAAATATGAATTTTAC
    GAAGGGATTGCTAAGGTAACAATAAATCGCCCTGAAGTACGCAATGCGTTTACACCTAAA
    ACAGTTGCTGAAATGATTGACGCATTTTCACGTGCACGTGATGATCAAAACGTTTCAGTT
    ATCGTATTAACTGGTGAAGGTGATTTAGCATTCTGTTCTGGTGGTGACCAGAAGAAACGT
    GGACATGGTGGTTATGTAGGTGAAGACCAAATCCCTCGCTTAAATGTATTAGATTTACAG
    CGTTTAATTCGTATTATTCCAAAACCGGTTATCGCGATGGTAAAAGGTTATGCTGTAGGT
    GGCGGTAATGTACTAAATGTTGTTTGTGACTTAACGATTGCTGCTGATAATGCTATTTTT
    GGACAAACTGGTCCTAAAGTAGGTTCATTTGATGCGGGTTATGGTTCAGGATATTTAGCA
    CGTATCGTTGGACATAAGAAAGCACGTGAAATTTGGTACTTATGTCGTCAATACAATGCA
    CAAGAAGCTTTAGATATGGGTCTAGTAAATACAGTGGTACCTTTAGAGAAAGTTGAAGAT
    GAAACTGTGCAATGGTGTAAAGAGATTATGAAACACTCACCAACAGCGTTACGATTCCTT
    AAAGCAGCTATGAATGCTGACACAGATGGTTTAGCTGGTTTACAACAAATGGCTGGGGAT
    GCAACATTGCTTTATTACACAACTGATGAAGCGAAAGAAGGCCGTGATGCGTTTAAAGAA
    AAACGTGATCCTGACTTCGATCAATTCCCTAAATTCCCATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    822

⊟Protein[edit | edit source]

Protein Data Bank: 2UZF

⊟General[edit | edit source]

  • locus tag: SAOUHSC_00985
  • symbol: SAOUHSC_00985
  • description: 1,4-dihydroxy-2-naphthoyl-CoA synthase
  • length: 273
  • theoretical pI: 5.23939
  • theoretical MW: 30425.4
  • GRAVY: -0.358608

⊟Function[edit | edit source]

  • reaction:
    EC 4.1.3.36?  ExPASy
    1,4-dihydroxy-2-naphthoyl-CoA synthase 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O
  • TIGRFAM:
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone naphthoate synthase (TIGR01929; EC 4.1.3.36; HMM-score: 424.3)
    and 9 more
    2-ketocyclohexanecarboxyl-CoA hydrolase (TIGR03210; EC 3.7.-.-; HMM-score: 315.5)
    phenylacetate degradation probable enoyl-CoA hydratase PaaB (TIGR02280; EC 4.2.1.17; HMM-score: 118.4)
    6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase (TIGR03200; EC 3.-.-.-; HMM-score: 101.6)
    Metabolism Fatty acid and phospholipid metabolism Degradation fatty oxidation complex, alpha subunit FadB (TIGR02437; EC 1.1.1.35,4.2.1.17,5.1.2.3,5.3.3.8; HMM-score: 56.8)
    cyclohexa-1,5-dienecarbonyl-CoA hydratase (TIGR03189; EC 4.2.1.100; HMM-score: 54.2)
    Metabolism Fatty acid and phospholipid metabolism Degradation fatty oxidation complex, alpha subunit FadJ (TIGR02440; EC 1.1.1.35,4.2.1.17,5.1.2.3; HMM-score: 48.2)
    fatty acid oxidation complex, alpha subunit, mitochondrial (TIGR02441; EC 1.1.1.35,4.2.1.17; HMM-score: 36.6)
    benzoyl-CoA-dihydrodiol lyase (TIGR03222; EC 4.1.2.44; HMM-score: 21.1)
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides signal peptide peptidase SppA, 36K type (TIGR00706; EC 3.4.-.-; HMM-score: 13.5)
  • TheSEED  :
    • Naphthoate synthase (EC 4.1.3.36)
    Cofactors, Vitamins, Prosthetic Groups, Pigments Quinone cofactors Menaquinone and Phylloquinone Biosynthesis  Naphthoate synthase (EC 4.1.3.36)
    and 1 more
    Cofactors, Vitamins, Prosthetic Groups, Pigments Quinone cofactors Menaquinone biosynthesis from chorismate via 1,4-dihydroxy-2-naphthoate  Naphthoate synthase (EC 4.1.3.36)
  • PFAM:
    ClpP_crotonase (CL0127) ECH_1; Enoyl-CoA hydratase/isomerase (PF00378; HMM-score: 298.6)
    and 5 more
    ECH_2; Enoyl-CoA hydratase/isomerase (PF16113; HMM-score: 76.4)
    NTF2 (CL0051) SnoaL_3; SnoaL-like domain (PF13474; HMM-score: 13.6)
    ClpP_crotonase (CL0127) Peptidase_S49; Peptidase family S49 (PF01343; HMM-score: 13.2)
    no clan defined DUF1666; Protein of unknown function (DUF1666) (PF07891; HMM-score: 12.7)
    ClpP_crotonase (CL0127) SDH_sah; Serine dehydrogenase proteinase (PF01972; HMM-score: 12.1)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • 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): 0.004575
    • TAT(Tat/SPI): 0.000519
    • LIPO(Sec/SPII): 0.000587
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTNRQWETLREYDEIKYEFYEGIAKVTINRPEVRNAFTPKTVAEMIDAFSRARDDQNVSVIVLTGEGDLAFCSGGDQKKRGHGGYVGEDQIPRLNVLDLQRLIRIIPKPVIAMVKGYAVGGGNVLNVVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEKVEDETVQWCKEIMKHSPTALRFLKAAMNADTDGLAGLQQMAGDATLLYYTTDEAKEGRDAFKEKRDPDFDQFPKFP

⊟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:

⊟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)

⊟Relevant publications[edit | edit source]

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