PtsH

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

Gene name	ptsH
Synonyms
Essential	no
Product	histidine-containing phosphocarrier protein HPr of the PTS
Function	PTS-dependent sugar transport and carbon catabolite repression
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism, Sugar catabolism
MW, pI	9,1 kDa, 4.58
Gene length, protein length	264 bp, 88 amino acids
Immediate neighbours	ptsG, ptsI
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU13900

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 (according to Swiss-Prot) Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine

• Protein family: HPr domain (according to Swiss-Prot) HPr family

• Paralogous protein(s): Crh

Extended information on the protein

• Kinetic information:

• Domains: HPr Domain (2–88)

• Modification: phosphorylations: transient phosphorylation by Enzyme I of the PTS on His-15, regulatory phosphorylation on Ser-46 by HprK PubMed, weak phosphorylation on Ser-12 PubMed, an extensive study on in vivo HPr phosphorylation can be found in Singh et al. (2008) PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:HPr-LicT, HPr-SacY, HPr-SacT, HPr-GlcT, HPr-GlpK, 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 (according to Swiss-Prot), Cytoplasm PubMed

Database entries

• Structure: 1KKM (complex of L. casei HprK with B. subtilis HPr-Ser-P), 1KKL (complex of Lactobacillus casei HprK with B. subtilis HPr), 2HID (NMR)

• Swiss prot entry: P08877

• KEGG entry: [3]

• E.C. number: 2.7.11.-

Expression and regulation

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

• Sigma factor: SigA PubMed

• Regulation: expression activated by glucose (2-fold) PubMed, induction by glucose (ptsG), constitutive (ptsH)

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

• Additional information:

Biological materials

• Mutant: MZ303 (cat), GP507 ptsH1 (S46A), GP506 (ptsH-H15A), available in Stülke lab

• Expression vector: pGP438 (with N-terminal Strep-tag, in pGP172), pAG2 (His-tag) pGP371(ptsH-S46A, with His-tag, in pWH844), available in Stülke

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Görke lab

• Antibody: available in Stülke lab

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. Reizer, J., Sutrina, S. L., Saier, Jr., M. H., Stewart, G. C., Peterkofsky, A., and Reddy, P. (1989) Mechanistic and physiological consequences of HPr(Ser) phosphorylation on the activities of the phosphoenolpyruvate:sugar phosphotransferase system in Gram-positive bacteria: studies with site-specific mutants of HPr. EMBO J 8: 2111-2120. PubMed
2. Schmalisch, M., Bachem, S. & Stülke, J. (2003) Control of the Bacillus subtilis antiterminator protein GlcT by phosphorylation: Elucidation of the phosphorylation chain leading to inactivation of GlcT. J. Biol. Chem. 278: 51108-51115. PubMed
3. Schumacher, M. A. et al. (2004) Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P. Cell 118, 731-741 . PubMed
4. Stülke, J., Martin-Verstraete, I., Charrier, V., Klier, A., Deutscher, J. & Rapoport, G. (1995) The HPr protein of the phosphotransferase system links induction and catabolite repression of the Bacillus subtilis levanase operon. J. Bacteriol. 177: 6928-6936. PubMed
5. Tortosa, P., Aymerich, S., Lindner, C., Saier, M.H., Jr., Reizer, J. and Le Coq, D. (1997) Multiple phosphorylation of SacY, a Bacillus subtilis antiterminator negatively controlled by the phosphotransferase system. J. Biol. Chem. 272, 17230-17237. PubMed
6. Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A (1997) 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 272:14166-14174. PubMed
7. Darbon E, Servant P, Poncet S, Deutscher J (2002) Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P~GlpK dephosphorylation control Bacillus subtilis glpFK expression. Mol Microbiol 43:1039-1052. PubMed
8. Jones, B.E., Rajagopal, P., and Klevit, R.E. (1997) Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis. Protein Sci 6: 2107-2119. PubMed
9. Rajagopal, P., Waygood, E.B., and Klevit, R.E. (1994) Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli. Biochemistry 33: 15271-15282. PubMed