PtsH

• Description: General component of the sugar phosphotransferase system (PTS).
  
  

Gene name	ptsH
Synonyms
Essential	no
Product	histidine-containing phosphocarrier protein of the PTS
Function	mediates carbon catabolite repression (CCR)
MW, pI	9,1 kDa, 4.58
Gene length, protein length	264 bp, 88 amino acids
Immediate neighbours	ptsG, ptsI
Gene sequence (+200bp)	Protein sequence
Genetic context

The gene

Basic information

• Coordinates: 1458693 - 1458956

Database entries

• DBTBS entry: [1]

• SubtiList entry:[2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine

• Protein family: HPr family

• Paralogous protein(s): Crh

Extended information on the protein

• Kinetic information:

• Domains: HPr Domain (2–88)

• Modification: phosphorylation (Ser-12)

• Cofactor(s):

• Effectors of protein activity:

• Interactions: GapA-HPr PubMed, HPr-MtlR, HPr-LicR, HPr-LevR,HPr-ManR, YesS-HPr (HPr-His-P), HPr-CcpA PubMed, HPr-RbsR PubMed, HprK-HPr PubMed

• Localization: Cytoplasm

Database entries

• Structure: NCBI, complex of L. Casei HprK with B. Subtilis HPr NCBI, complex of L. Casei HprK with B. Subtilis HPr-Ser-P NCBI

• Swiss prot entry: [3]

• KEGG entry: [4]

• E.C. number: [5]

Expression and regulation

• Operon:
  • ptsG-ptsH-ptsI
  • ptsH-ptsI

• Sigma factor: SigA PubMed

• Regulation: induction by glucose (ptsG), constitutive (ptsH)

• Regulatory mechanism: ptsG: transcriptional antitermination via the GlcT-dependent RNA-switch

• Additional information:

Labs working on this gene/protein

Josef Deutscher, Paris-Grignon, France

Jörg Stülke, University of Göttingen, Germany Homepage

Wolfgang Hillen, Erlangen University, Germany Homepage

Richard Brennan, Houston, Texas, USA Homepage

Boris Görke, University of Göttingen, Germany Homepage

Anne Galinier, University of Marseille, France

References

1. Macek B, Mijakovic I, Olsen JV (2007) The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics 6(4): 697-707. PubMed
2. Mahr K, Esteban CD, Hillen W (2002) Cross communication between components of carbon catabolite repression of Lactobacillus casei and Bacillus megaterium. J Mol Microbiol Biotechnol. 4(5): 489-94. PubMed
3. Juy M, Penin F, Favier A, Galinier 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
4. Müller W, Horstmann N, Hillen W (2006) The transcription regulator RbsR represents a novel interaction partner of the phosphoprotein HPr-Ser46-P in Bacillus subtilis FEBS J. 273(6): 1251-61. PubMed
5. Lavergne JP, Jault JM, Galinier A (2002) Insights into the functioning of Bacillus subtilis HPr kinase/phosphatase: affinity for its protein substrates and role of cations and phosphate Biochemistry 41(20): 6218-25. 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