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Description: "Carbon-flux regulating HPr", formerly known as "Catabolite repression HPr-like protein", control of flux through the harmful methylglyoxal pathway, minor cofactor of the CcpA transcription factor

Name: crh
Locus: BSU34740BsubCyc
pI: 4.7
MW: 9.2 kDa
Protein length: 85 aaBLASTSequence
Gene length: 255 bpBLASTSequenceSequence + Flanks
Function: control of carbon flux
Product: carbon-flux regulating HPr
Essential: no
E.C. number:
Synonyms: yvcM
Databases: SubtiListKEGGUniProtExpression data browser

Categories containing this gene/protein

transcription factors and their control, phosphoproteins

This gene is a member of the following regulons


  • Coordinates on the chromosome (coding sequence): 3,569,292 -> 3,569,549
  • The protein

    Catalyzed reaction/ biological activity

    Protein family

  • HPr family
  • Paralogous protein(s)

  • HPr
  • Kinetic information


  • HPr domain (1–85)
  • Modification

  • phosphorylation on Ser46 by HprK PubMed
  • Cofactors

    Effectors of protein activity


  • 2AK7 (dimeric Crh-Ser46-P)
  • 1ZVV (CcpA-Crh-DNA complex)
  • 2RLZ (dimer)
  • 1MU4
  • NCBI, dimer
  • NCBI, CcpA-Crh-DNA complex
  • NCBI, dimeric phosphor-Crh
  • NCBI
  • Localization


  • Crh-GapA PubMed
  • Crh-CcpA PubMed
  • HprK-Crh PubMed
  • Crh-MgsA (only non-phosphorylated Crh interacts with MgsA) PubMed
  • Additional information

  • Crh does not possess the phosphorylation site used for PTS phosphotransfer (His-15 in PtsH), it can only be phosphorylated on Ser-46
  • Expression and Regulation


  • yvcI-yvcJ-yvcK-yvcL-crh-yvcN PubMed
  • Sigma factor

  • SigA PubMed
  • Regulation

  • very weak stimuation of expression by citrate and succinate PubMed
  • Regulatory mechanism

    Additional information

  • Crh is weakly expressed. This results in part from a poorly conserved ribosomal binding site of the mRNA. PubMed
  • Biological materials


  • GP860 (aphA3) PubMed, QB7097 (spc), available in Jörg Stülke's lab
  • Expression vector

  • pGP641 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Jörg Stülke's lab
  • pGP734 (C-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP382), available in Jörg Stülke's lab
  • lacZ fusion

  • see yvcI
  • GFP fusion

    two-hybrid system

  • crh, crh(Ser46Asp), crh(Ser46Ala) B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • FLAG-tag construct


    Labs working on this gene/protein

  • Boris Görke, University of Göttingen, Germany
  • Homepage
  • Anne Galinier, University of Marseille, France
  • Wolfgang Hillen, Erlangen University, Germany Homepage
  • Richard Brennan, Houston, Texas, USA Homepage
  • References

    Landmann JJ, Werner S, Hillen W, Stülke J, Görke B

    Carbon source control of the phosphorylation state of the Bacillus subtilis carbon-flux regulator Crh in vivo

    FEMS Microbiol Lett. 2012 Feb;327(1):47-53. doi: 10.1111/j.1574-6968.2011.02456.x. Epub 2011 Nov 28. PubMed PMID: 22092971.
    Landmann JJ, Busse RA, Latz JH, Singh KD, Stülke J, Görke B

    Crh, the paralogue of the phosphocarrier protein HPr, controls the methylglyoxal bypass of glycolysis in Bacillus subtilis

    Mol Microbiol. 2011 Nov;82(3):770-87. doi: 10.1111/j.1365-2958.2011.07857.x. Epub 2011 Oct 12. PubMed PMID: 21992469.
    Gardiennet C, Loquet A, Etzkorn M, Heise H, Baldus M, Böckmann A

    Structural constraints for the Crh protein from solid-state NMR experiments

    J Biomol NMR. 2008 Apr;40(4):239-50. doi: 10.1007/s10858-008-9229-3. Epub 2008 Mar 5. PubMed PMID: 18320329; PubMed Central PMCID: PMC2579321.
    Loquet A, Bardiaux B, Gardiennet C, Blanchet C, Baldus M, Nilges M, Malliavin T, Böckmann A

    3D structure determination of the Crh protein from highly ambiguous solid-state NMR restraints

    J Am Chem Soc. 2008 Mar 19;130(11):3579-89. doi: 10.1021/ja078014t. Epub 2008 Feb 20. PubMed PMID: 18284240.
    Pompeo F, Luciano J, Galinier A

    Interaction of GapA with HPr and its homologue, Crh: Novel levels of regulation of a key step of glycolysis in Bacillus subtilis

    J Bacteriol. 2007 Feb;189(3):1154-7. Epub 2006 Dec 1. PubMed PMID: 17142398; PubMed Central PMCID: PMC1797305.
    Chaptal V, Larivière L, Gueguen-Chaignon V, Galinier A, Nessler S, Moréra S

    X-ray structure of a domain-swapped dimer of Ser46-phosphorylated Crh from Bacillus subtilis

    Proteins. 2006 Apr 1;63(1):249-51. PubMed PMID: 16411239.
    Schumacher MA, Seidel G, Hillen W, Brennan RG

    Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation

    J Biol Chem. 2006 Mar 10;281(10):6793-800. Epub 2005 Nov 29. PubMed PMID: 16316990.
    Görke B, Foulquier E, Galinier A

    YvcK of Bacillus subtilis is required for a normal cell shape and for growth on Krebs cycle intermediates and substrates of the pentose phosphate pathway

    Microbiology. 2005 Nov;151(Pt 11):3777-91. PubMed PMID: 16272399.
    Görke B, Fraysse L, Galinier A

    Drastic differences in Crh and HPr synthesis levels reflect their different impacts on catabolite repression in Bacillus subtilis

    J Bacteriol. 2004 May;186(10):2992-5. PubMed PMID: 15126459; PubMed Central PMCID: PMC400640.
    Juy M, Penin F, Favier A, Galinier A, Montserret R, Haser R, Deutscher J, Böckmann A

    Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr

    J Mol Biol. 2003 Sep 26;332(4):767-76. PubMed PMID: 12972249.
    Warner JB, Lolkema JS

    A Crh-specific function in carbon catabolite repression in Bacillus subtilis

    FEMS Microbiol Lett. 2003 Mar 28;220(2):277-80. PubMed PMID: 12670692.
    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.
    Favier A, Brutscher B, Blackledge M, Galinier A, Deutscher J, Penin F, Marion D

    Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr

    J Mol Biol. 2002 Mar 15;317(1):131-44. PubMed PMID: 11916384.
    Darbon E, Galinier A, Le Coq D, Deutscher J

    Phosphotransfer functions mutated Bacillus subtilis HPr-like protein Crh carrying a histidine in the active site

    J Mol Microbiol Biotechnol. 2001 Jul;3(3):439-44. Review. PubMed PMID: 11361076.
    Penin F, Favier A, Montserret R, Brutscher B, Deutscher J, Marion D, Galinier D

    Evidence for a dimerisation state of the Bacillus subtilis catabolite repression HPr-like protein, Crh

    J Mol Microbiol Biotechnol. 2001 Jul;3(3):429-32. PubMed PMID: 11361074.
    Martin-Verstraete I, Galinier A, Darbon E, Quentin Y, Kilhoffer MC, Charrier V, Haiech J, Rapoport G, Deutscher J

    The Q15H mutation enables Crh, a Bacillus subtilis HPr-like protein, to carry out some regulatory HPr functions, but does not make it an effective phosphocarrier for sugar transport

    Microbiology. 1999 Nov;145 ( Pt 11):3195-204. PubMed PMID: 10589728.
    Martin-Verstraete I, Deutscher J, Galinier A

    Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon

    J Bacteriol. 1999 May;181(9):2966-9. PubMed PMID: 10217795; PubMed Central PMCID: PMC93746.
    Galinier A, Deutscher J, Martin-Verstraete I

    Phosphorylation of either crh or HPr mediates binding of CcpA to the bacillus subtilis xyn cre and catabolite repression of the xyn operon

    J Mol Biol. 1999 Feb 19;286(2):307-14. PubMed PMID: 9973552.
    Galinier A, Haiech J, Kilhoffer MC, Jaquinod M, Stülke J, Deutscher J, Martin-Verstraete I

    The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression

    Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8439-44. PubMed PMID: 9237995; PubMed Central PMCID: PMC22949.
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