Difference between revisions of "PtsH"

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<pubmed>16519689,,12850135 17218307 16519689 17142398 12359875 1577686 9162046 11929549 9336834 7803390, 7623661, 2846556, 8169206, 9973552, 15126459, 10048041, 12169607, 9622354, 10217795, 17693724, 18757537 , 9202047 , 7592487, 15369672 , 14527945, 2507315 </pubmed>
 
<pubmed>16519689,,12850135 17218307 16519689 17142398 12359875 1577686 9162046 11929549 9336834 7803390, 7623661, 2846556, 8169206, 9973552, 15126459, 10048041, 12169607, 9622354, 10217795, 17693724, 18757537 , 9202047 , 7592487, 15369672 , 14527945, 2507315 </pubmed>
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[[Category:Protein-coding genes]]

Revision as of 09:53, 21 July 2009

  • 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
PtsH context.gif
This image was kindly provided by SubtiList








The gene

Basic information

  • Locus tag: BSU13900

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry:[2]

Additional information

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:
  • 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)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

Your additional remarks

References

Kalpana D Singh, Matthias H Schmalisch, Jörg Stülke, Boris Görke
Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources.
J Bacteriol: 2008, 190(21);7275-84
[PubMed:18757537] [WorldCat.org] [DOI] (I p)

Kalpana D Singh, Sven Halbedel, Boris Görke, Jörg Stülke
Control of the phosphorylation state of the HPr protein of the phosphotransferase system in Bacillus subtilis: implication of the protein phosphatase PrpC.
J Mol Microbiol Biotechnol: 2007, 13(1-3);165-71
[PubMed:17693724] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Frédérique Pompeo, Jennifer Luciano, Anne Galinier
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, 189(3);1154-7
[PubMed:17142398] [WorldCat.org] [DOI] (P p)

Wolfgang Müller, Nicola Horstmann, Wolfgang Hillen, Heinrich Sticht
The transcription regulator RbsR represents a novel interaction partner of the phosphoprotein HPr-Ser46-P in Bacillus subtilis.
FEBS J: 2006, 273(6);1251-61
[PubMed:16519689] [WorldCat.org] [DOI] (P p)

Maria A Schumacher, Gregory S Allen, Marco Diel, Gerald Seidel, Wolfgang Hillen, Richard G Brennan
Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P.
Cell: 2004, 118(6);731-41
[PubMed:15369672] [WorldCat.org] [DOI] (P p)

Boris Görke, Laetitia Fraysse, Anne Galinier
Drastic differences in Crh and HPr synthesis levels reflect their different impacts on catabolite repression in Bacillus subtilis.
J Bacteriol: 2004, 186(10);2992-5
[PubMed:15126459] [WorldCat.org] [DOI] (P p)

Matthias H Schmalisch, Steffi Bachem, Jörg Stülke
Control of the Bacillus subtilis antiterminator protein GlcT by phosphorylation. Elucidation of the phosphorylation chain leading to inactivation of GlcT.
J Biol Chem: 2003, 278(51);51108-15
[PubMed:14527945] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Sonia Fieulaine, Solange Morera, Sandrine Poncet, Ivan Mijakovic, Anne Galinier, Joël Janin, Josef Deutscher, Sylvie Nessler
X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr.
Proc Natl Acad Sci U S A: 2002, 99(21);13437-41
[PubMed:12359875] [WorldCat.org] [DOI] (P p)

Cordula Lindner, Michael Hecker, Dominique Le Coq, Josef Deutscher
Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon.
J Bacteriol: 2002, 184(17);4819-28
[PubMed:12169607] [WorldCat.org] [DOI] (P p)

Emmanuelle Darbon, Pascale Servant, Sandrine Poncet, Josef Deutscher
Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression.
Mol Microbiol: 2002, 43(4);1039-52
[PubMed:11929549] [WorldCat.org] [DOI] (P p)

I Martin-Verstraete, J Deutscher, A Galinier
Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon.
J Bacteriol: 1999, 181(9);2966-9
[PubMed:10217795] [WorldCat.org] [DOI] (P p)

C Lindner, A Galinier, M Hecker, J Deutscher
Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation.
Mol Microbiol: 1999, 31(3);995-1006
[PubMed:10048041] [WorldCat.org] [DOI] (P p)

A Galinier, J Deutscher, I Martin-Verstraete
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(2);307-14
[PubMed:9973552] [WorldCat.org] [DOI] (P p)

I Martin-Verstraete, V Charrier, J Stülke, A Galinier, B Erni, G Rapoport, J Deutscher
Antagonistic effects of dual PTS-catalysed phosphorylation on the Bacillus subtilis transcriptional activator LevR.
Mol Microbiol: 1998, 28(2);293-303
[PubMed:9622354] [WorldCat.org] [DOI] (P p)

B E Jones, P Rajagopal, R E Klevit
Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis.
Protein Sci: 1997, 6(10);2107-19
[PubMed:9336834] [WorldCat.org] [DOI] (P p)

P Tortosa, S Aymerich, C Lindner, M H Saier, J Reizer, D Le Coq
Multiple phosphorylation of SacY, a Bacillus subtilis transcriptional antiterminator negatively controlled by the phosphotransferase system.
J Biol Chem: 1997, 272(27);17230-7
[PubMed:9202047] [WorldCat.org] [DOI] (P p)

V Charrier, E Buckley, D Parsonage, A Galinier, E Darbon, M Jaquinod, E Forest, J Deutscher, A Claiborne
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: 1997, 272(22);14166-74
[PubMed:9162046] [WorldCat.org] [DOI] (P p)

J Stülke, I Martin-Verstraete, V Charrier, A Klier, J Deutscher, G Rapoport
The HPr protein of the phosphotransferase system links induction and catabolite repression of the Bacillus subtilis levanase operon.
J Bacteriol: 1995, 177(23);6928-36
[PubMed:7592487] [WorldCat.org] [DOI] (P p)

J Deutscher, E Küster, U Bergstedt, V Charrier, W Hillen
Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in gram-positive bacteria.
Mol Microbiol: 1995, 15(6);1049-53
[PubMed:7623661] [WorldCat.org] [DOI] (P p)

P Rajagopal, E B Waygood, R E Klevit
Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli.
Biochemistry: 1994, 33(51);15271-82
[PubMed:7803390] [WorldCat.org] [DOI] (P p)

D Frisby, P Zuber
Mutations in pts cause catabolite-resistant sporulation and altered regulation of spo0H in Bacillus subtilis.
J Bacteriol: 1994, 176(9);2587-95
[PubMed:8169206] [WorldCat.org] [DOI] (P p)

M Arnaud, P Vary, M Zagorec, A Klier, M Debarbouille, P Postma, G Rapoport
Regulation of the sacPA operon of Bacillus subtilis: identification of phosphotransferase system components involved in SacT activity.
J Bacteriol: 1992, 174(10);3161-70
[PubMed:1577686] [WorldCat.org] [DOI] (P p)

J Reizer, S L Sutrina, M H Saier, G C Stewart, A Peterkofsky, P Reddy
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: 1989, 8(7);2111-20
[PubMed:2507315] [WorldCat.org] [DOI] (P p)

R Eisermann, J Deutscher, G Gonzy-Treboul, W Hengstenberg
Site-directed mutagenesis with the ptsH gene of Bacillus subtilis. Isolation and characterization of heat-stable proteins altered at the ATP-dependent regulatory phosphorylation site.
J Biol Chem: 1988, 263(32);17050-4
[PubMed:2846556] [WorldCat.org] (P p)

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