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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1054 [new locus tag: SACOL_RS05375 ]
  • pan locus tag?: SAUPAN003248000
  • symbol: menB
  • pan gene symbol?: menB
  • synonym:
  • product: naphthoate synthase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1054 [new locus tag: SACOL_RS05375 ]
  • symbol: menB
  • product: naphthoate synthase
  • replicon: chromosome
  • strand: +
  • coordinates: 1060326..1061147
  • length: 822
  • 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
    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: SACOL1054 [new locus tag: SACOL_RS05375 ]
  • symbol: MenB
  • description: naphthoate 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: 295.6)
    and 4 more
    ECH_2; Enoyl-CoA hydratase/isomerase (PF16113; HMM-score: 78.2)
    Peptidase_S49; Peptidase family S49 (PF01343; HMM-score: 13.6)
    no clan defined DUF1666; Protein of unknown function (DUF1666) (PF07891; HMM-score: 12.4)
    ClpP_crotonase (CL0127) SDH_protease; ClpP-like SDH-type serine 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
  • ⊞DeepLocPro: Cytoplasmic
    • Cytoplasmic Score: 0.9406
    • Cytoplasmic Membrane Score: 0.0419
    • Cell wall & surface Score: 0
    • Extracellular Score: 0.0175
  • ⊞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
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1004 [5]
  • 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. ↑ 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)

⊟Relevant publications[edit | edit source]

Venkatasubramanian Ulaganathan, Mark F Agacan, Lori Buetow, Lindsay B Tulloch, William N Hunter
Structure of Staphylococcus aureus1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) in complex with acetoacetyl-CoA.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2007, 63(Pt 11);908-13
[PubMed:18007038] [WorldCat.org] [DOI] (I p)Ming Jiang, Minjiao Chen, Zu-Feng Guo, Zhihong Guo
A bicarbonate cofactor modulates 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase in menaquinone biosynthesis of Escherichia coli.
J Biol Chem: 2010, 285(39);30159-69
[PubMed:20643650] [WorldCat.org] [DOI] (I p)

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