Crh

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  • Description: "Catabolite rpression HPr-like protein", Cofactor of the CcpA transcription factor

Gene name crh
Synonyms yvcM
Essential no
Product catabolite repression HPr-like protein
Function catabolite repression
MW, pI 9,2 kDa, 4.70
Gene length, protein length 255 bp, 85 amino acids
Immediate neighbours yvcL, yvcN
Gene sequence (+200bp) Protein sequence
Genetic context
Crh context.gif



The gene

Basic information

  • Coordinates: 3568325 - 3568579

Phenotypes of a mutant

Database entries

  • DBTBS entry:
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: PtsH,HPr family
  • Paralogous protein(s): HPr

Extended information on the protein

  • Kinetic information:
  • Domains: HPr domain (1–85)
  • Modification: phosphorylation at Ser46 by HPrK
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:

Database entries

  • Structure: NCBI, dimer NCBI, CcpA-Crh-DNA complex NCBI, dimeric phosphor-Crh NCBI
  • Swiss prot entry: [2]
  • KEGG entry: [3]

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

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP860 (aphA3), QB7097 (spc), available in Stülke lab
  • Expression vector: pGP641 (in pGP380, for SPINE, expression in B. subtilis), pGP734 (in pGP380, for SPINE, expression in B. subtilis), available in Stülke lab
  • lacZ fusion: see yvcI
  • GFP fusion:
  • Antibody: available in Stülke lab (not very good)

Labs working on this gene/protein

Boris Görke, University of Göttingen, Germany Homepage

Anne Galinier, University of Marseille, France

Your additional remarks

References

  1. Juy M, Penin F, Favier A (2003) Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr. J Mol Biol. 332(4):767-76. PubMed
  2. 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, 286:307-314. PubMed
  3. Galinier, A., Haiech, J., Kilhoffer, M.-C., Jaquinod, M., Stülke, J., Deutscher, J., & Martin-Verstraete, I. (1997) The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression. Proc. Natl. Acad. Sci. USA 94: 8439-8444. PubMed
  4. 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. 186, 2992-2995 (2004). PubMed
  5. Martin-Verstraete, I., Deutscher, J., and Galinier, A. (1999) Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon. J Bacteriol 181: 2966-2969. PubMed
  6. Pompeo et al. (2007) Interaction of GapA with HPr and its homologue, Crh: Novel levels of regulation of a key step of glycolysis in Bacillus subtilis? J Bacteriol 189, 1154-1157.PubMed
  7. Schumacher, M. A., Seidel, G., Hillen, W. & Brennan, R. G. Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation. J. Biol. Chem. 281, 6793-6800 (2006). PubMed