SubtiBank SubtiBank

Categories containing this gene/protein


utilization of specific carbon sources, phosphoproteins

This gene is a member of the following regulons


AbrB regulon, CcpA regulon, GlpP regulon

Gene


  • Coordinates on the chromosome (coding sequence): 1,003,344 -> 1,004,834
  • The protein


    Catalyzed reaction/ biological activity

  • ATP + glycerol = ADP + sn-glycerol 3-phosphate (according to Swiss-Prot)
  • Protein family

  • FGGY kinase family (according to Swiss-Prot)
  • Paralogous protein(s)

    Kinetic information

    Domains

    Modification

    Cofactors

    Effectors of protein activity

    Structure

  • 3H46 (from Enterococcus casseliflavus, complex with glycerol) PubMed
  • Localization

    Interactions

  • PtsH-GlpK
  • Additional information

    Expression and Regulation


    Operon

  • glpF-glpK PubMed
  • Sigma factor

  • SigA PubMed
  • Regulation

  • repressed by glucose (8-fold) (CcpA) PubMed
  • induction by glycerol (GlpP) PubMed
  • Regulatory mechanism

  • CcpA: transcription repression PubMed
  • GlpP-dependent RNA switch (transcriptional antitermination) PubMed
  • AbrB: transcription activation PubMed
  • Additional information

    Biological materials


    Mutant

  • BKE09290 (glpK::ermC) (available at the BGSC and in Jörg Stülke's lab)
  • GP1865 (glpK::ermC) (available in Jörg Stülke's lab)
  • Expression vector

    lacZ fusion

    GFP fusion

    two-hybrid system

    FLAG-tag construct

    Antibody

    Labs working on this gene/protein


  • Josef Deutscher, Paris-Grignon, France
  • References


    Chumsakul O, Takahashi H, Oshima T, Hishimoto T, Kanaya S, Ogasawara N, Ishikawa S

    Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation

    Nucleic Acids Res. 2011 Jan;39(2):414-28. doi: 10.1093/nar/gkq780. Epub 2010 Sep 3. PubMed PMID: 20817675; PubMed Central PMCID: PMC3025583.
    Yeh JI, Kettering R, Saxl R, Bourand A, Darbon E, Joly N, Briozzo P, Deutscher J

    Structural characterizations of glycerol kinase: unraveling phosphorylation-induced long-range activation

    Biochemistry. 2009 Jan 20;48(2):346-56. doi: 10.1021/bi8009407. PubMed PMID: 19102629; PubMed Central PMCID: PMC3158585.
    Darbon E, Servant P, Poncet S, Deutscher J

    Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression

    Mol Microbiol. 2002 Feb;43(4):1039-52. PubMed PMID: 11929549.
    Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A

    Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue

    J Biol Chem. 1997 May 30;272(22):14166-74. PubMed PMID: 9162046.
    Wehtje C, Beijer L, Nilsson RP, Rutberg B

    Mutations in the glycerol kinase gene restore the ability of a ptsGHI mutant of Bacillus subtilis to grow on glycerol

    Microbiology. 1995 May;141 ( Pt 5):1193-8. PubMed PMID: 7773413.
    Beijer L, Rutberg L

    Utilisation of glycerol and glycerol 3-phosphate is differently affected by the phosphotransferase system in Bacillus subtilis

    FEMS Microbiol Lett. 1992 Dec 15;100(1-3):217-20. PubMed PMID: 1335945.
    No login