SubtiBank SubtiBank

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Categories containing this gene/protein

protein modification, transcription factors and their control

This gene is a member of the following regulons


  • Coordinates on the chromosome (coding sequence): 3,594,242 -> 3,595,174
  • Phenotypes of a mutant

  • no carbon catabolite repression PubMed
  • delay in spore germination PubMed
  • The protein

    Catalyzed reaction/ biological activity

  • ATP HPr = ADP P-Ser-HPr (according to Swiss-Prot)
  • Protein family

  • HPrK/P family (according to Swiss-Prot)
  • Paralogous protein(s)

    Kinetic information




    Effectors of protein activity


  • 1KKM (complex of Lactobacillus casei HprK with B. subtilis HPr-Ser-P), 1KKL (complex of Lactobacillus casei HprK with B. subtilis HPr)
  • Localization


  • HprK-HPr
  • HprK-Crh PubMed
  • Additional information

    Expression and Regulation


  • hprK-lgt-yvoD-yvoE-yvoF PubMed
  • Sigma factor

  • SigA PubMed
  • Regulation

    Regulatory mechanism

    Additional information

    Biological materials


  • MGNA-A328 (yvoB::erm), available at the NBRP B. subtilis, Japan
  • GP202 (spc) PubMed, GP858 (aphA3) PubMed, GP82 (cat) PubMed, all available in Jörg Stülke's lab
  • Expression vector

  • for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP642, available in Jörg Stülke's lab
  • for expression/ purification of mutant HprK-G158A from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP650, available in Jörg Stülke's lab
  • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP205, available in Jörg Stülke's lab
  • for expression, purification of the N-terminal in E. coli with N-terminal His-tag, in pWH844: pGP218, available in Jörg Stülke's lab
  • lacZ fusion

  • pGP201 (in pAC5, PubMed) available in Stülke lab, pGP202 (in pAC6, PubMed) available in Jörg Stülke's lab
  • GFP fusion

    two-hybrid system

    FLAG-tag construct


  • available in Jörg Stülke's lab PubMed
  • Labs working on this gene/protein

  • Josef Deutscher, Paris-Grignon, France
  • Jörg Stülke, University of Göttingen, Germany Homepage
  • Wolfgang Hillen, Erlangen University, Germany Homepage
  • Anne Galinier, University of Marseille, France
  • References


    Görke B, Stülke J

    Carbon catabolite repression in bacteria: many ways to make the most out of nutrients

    Nat Rev Microbiol. 2008 Aug;6(8):613-24. doi: 10.1038/nrmicro1932. Review. PubMed PMID: 18628769.
    Poncet S, Mijakovic I, Nessler S, Gueguen-Chaignon V, Chaptal V, Galinier A, Boël G, Mazé A, Deutscher J

    HPr kinase/phosphorylase, a Walker motif A-containing bifunctional sensor enzyme controlling catabolite repression in Gram-positive bacteria

    Biochim Biophys Acta. 2004 Mar 11;1697(1-2):123-35. Review. PubMed PMID: 15023355.
    Nessler S, Fieulaine S, Poncet S, Galinier A, Deutscher J, Janin J

    HPr kinase/phosphorylase, the sensor enzyme of catabolite repression in Gram-positive bacteria: structural aspects of the enzyme and the complex with its protein substrate

    J Bacteriol. 2003 Jul;185(14):4003-10. PubMed PMID: 12837773; PubMed Central PMCID: PMC164879.

    General Analysis, Physiology

    Rosenberg A, Soufi B, Ravikumar V, Soares NC, Krug K, Smith Y, Macek B, Ben-Yehuda S

    Phosphoproteome dynamics mediate revival of bacterial spores

    BMC Biol. 2015 Sep 17;13:76. doi: 10.1186/s12915-015-0184-7. PubMed PMID: 26381121; PubMed Central PMCID: PMC4574613.
    Gaugué I, Oberto J, Putzer H, Plumbridge J

    The use of amino sugars by Bacillus subtilis: presence of a unique operon for the catabolism of glucosamine

    PLoS One. 2013 May 8;8(5):e63025. doi: 10.1371/journal.pone.0063025. Print 2013. PubMed PMID: 23667565; PubMed Central PMCID: PMC3648570.
    Meyer FM, Jules M, Mehne FM, Le Coq D, Landmann JJ, Görke B, Aymerich S, Stülke J

    Malate-mediated carbon catabolite repression in Bacillus subtilis involves the HPrK/CcpA pathway

    J Bacteriol. 2011 Dec;193(24):6939-49. doi: 10.1128/JB.06197-11. Epub 2011 Oct 14. PubMed PMID: 22001508; PubMed Central PMCID: PMC3232832.
    Singh KD, Schmalisch MH, Stülke J, Görke B

    Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources

    J Bacteriol. 2008 Nov;190(21):7275-84. doi: 10.1128/JB.00848-08. Epub 2008 Aug 29. PubMed PMID: 18757537; PubMed Central PMCID: PMC2580719.
    Ludwig H, Rebhan N, Blencke HM, Merzbacher M, Stülke J

    Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation

    Mol Microbiol. 2002 Jul;45(2):543-53. PubMed PMID: 12123463.
    Reizer J, Hoischen C, Titgemeyer F, Rivolta C, Rabus R, Stülke J, Karamata D, Saier MH Jr, Hillen W

    A novel protein kinase that controls carbon catabolite repression in bacteria

    Mol Microbiol. 1998 Mar;27(6):1157-69. PubMed PMID: 9570401.
    Galinier A, Kravanja M, Engelmann R, Hengstenberg W, Kilhoffer MC, Deutscher J, Haiech J

    New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression

    Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1823-8. PubMed PMID: 9465101; PubMed Central PMCID: PMC19197.

    Structural Analysis of HPrK

    Chaptal V, Vincent F, Gueguen-Chaignon V, Monedero V, Poncet S, Deutscher J, Nessler S, Morera S

    Structural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzyme

    J Biol Chem. 2007 Nov 30;282(48):34952-7. Epub 2007 Sep 18. PubMed PMID: 17878158.
    Allen GS, Steinhauer K, Hillen W, Stülke J, Brennan RG

    Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae

    J Mol Biol. 2003 Feb 28;326(4):1203-17. PubMed PMID: 12589763.
    Fieulaine S, Morera S, Poncet S, Mijakovic I, Galinier A, Janin J, Deutscher J, Nessler S

    X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr

    Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13437-41. Epub 2002 Oct 1. PubMed PMID: 12359875; PubMed Central PMCID: PMC129691.
    Márquez JA, Hasenbein S, Koch B, Fieulaine S, Nessler S, Russell RB, Hengstenberg W, Scheffzek K

    Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1

    95 A resolution: Mimicking the product/substrate of the phospho transfer reactions. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3458-63. PubMed PMID: 11904409; PubMed Central PMCID: PMC122545.

    Enzymatic Properties, Mutation Analysis

    Pompeo F, Granet Y, Lavergne JP, Grangeasse C, Nessler S, Jault JM, Galinier A

    Regulation and mutational analysis of the HPr kinase/phosphorylase from Bacillus subtilis

    Biochemistry. 2003 Jun 10;42(22):6762-71. PubMed PMID: 12779331.
    Ramström H, Sanglier S, Leize-Wagner E, Philippe C, Van Dorsselaer A, Haiech J

    Properties and regulation of the bifunctional enzyme HPr kinase/phosphatase in Bacillus subtilis

    J Biol Chem. 2003 Jan 10;278(2):1174-85. Epub 2002 Oct 30. PubMed PMID: 12411438.
    Mijakovic I, Poncet S, Galinier A, Monedero V, Fieulaine S, Janin J, Nessler S, Marquez JA, Scheffzek K, Hasenbein S, Hengstenberg W, Deutscher J

    Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: a relic of early life

    Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13442-7. Epub 2002 Oct 1. PubMed PMID: 12359880; PubMed Central PMCID: PMC129692.
    Hanson KG, Steinhauer K, Reizer J, Hillen W, Stülke J

    HPr kinase/phosphatase of Bacillus subtilis: expression of the gene and effects of mutations on enzyme activity, growth and carbon catabolite repression

    Microbiology. 2002 Jun;148(Pt 6):1805-11. PubMed PMID: 12055300.
    Lavergne JP, Jault JM, Galinier A

    Insights into the functioning of Bacillus subtilis HPr kinase/phosphatase: affinity for its protein substrates and role of cations and phosphate

    Biochemistry. 2002 May 21;41(20):6218-25. PubMed PMID: 12009882.
    Galinier A, Lavergne JP, Geourjon C, Fieulaine S, Nessler S, Jault JM

    A new family of phosphotransferases with a P-loop motif

    J Biol Chem. 2002 Mar 29;277(13):11362-7. Epub 2002 Jan 16. PubMed PMID: 11796714.
    Monedero V, Poncet S, Mijakovic I, Fieulaine S, Dossonnet V, Martin-Verstraete I, Nessler S, Deutscher J

    Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism

    EMBO J. 2001 Aug 1;20(15):3928-37. PubMed PMID: 11483496; PubMed Central PMCID: PMC149165.
    Jault JM, Fieulaine S, Nessler S, Gonzalo P, Di Pietro A, Deutscher J, Galinier A

    The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding

    J Biol Chem. 2000 Jan 21;275(3):1773-80. PubMed PMID: 10636874.

    HprK as a Target For Antimicrobial Compounds

    Ramström H(1), Bourotte M, Philippe C, Schmitt M, Haiech J, Bourguignon JJ.

    Heterocyclic bis-cations as starting hits for design of inhibitors of the bifunctional enzyme histidine-containing protein kinase/phosphatase from Bacillus subtilis.

    J Med Chem. 2004 Apr 22;47(9):2264-75.
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