Difference between revisions of "HprK"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hprK_3594242_3595174_-1 hprK] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hprK_3594242_3595174_-1 hprK] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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==General Analysis, Physiology==
 
==General Analysis, Physiology==
<pubmed>9570401 9465101 12123463 18757537 22001508 </pubmed>
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==Structural Analysis of HPrK==
 
==Structural Analysis of HPrK==

Revision as of 16:48, 24 May 2013

Gene name hprK
Synonyms ptsK, yvoB
Essential no
Product HPr kinase/ phosphorylase
Function carbon catabolite repression,
phosphorylation of HPr and Crh proteins at Ser46
Gene expression levels in SubtiExpress: hprK
Interactions involving this protein in SubtInteract: HprK
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism, Protein secretion
MW, pI 34 kDa, 4.906
Gene length, protein length 930 bp, 310 aa
Immediate neighbours lgt, nagA
Sequences Protein DNA DNA_with_flanks
Genetic context
HprK context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
HprK expression.png















Categories containing this gene/protein

protein modification, transcription factors and their control

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU35000

Phenotypes of a mutant

no carbon catabolite repression

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + HPr = ADP + P-Ser-HPr (according to Swiss-Prot)
  • Protein family: HPrK/P family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1KKM (complex of Lactobacillus casei HprK with B. subtilis HPr-Ser-P), 1KKL (complex of Lactobacillus casei HprK with B. subtilis HPr)
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP202 (spc), GP858 (aphA3), GP82 (cat), available in Stülke lab
  • Expression vector:
    • for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP642, available in Stülke lab
    • for expression/ purification of mutant HprK-G158A from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP650, available in Stülke lab
    • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP205, available in Stülke lab
    • for expression, purification of the N-terminal in E. coli with N-terminal His-tag, in pWH844: pGP218, available in Stülke lab
  • GFP fusion:
  • two-hybrid system:
  • 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

Anne Galinier, University of Marseille, France

Your additional remarks

References

Reviews

Boris Görke, Jörg Stülke
Carbon catabolite repression in bacteria: many ways to make the most out of nutrients.
Nat Rev Microbiol: 2008, 6(8);613-24
[PubMed:18628769] [WorldCat.org] [DOI] (I p)

Sandrine Poncet, Ivan Mijakovic, Sylvie Nessler, Virginie Gueguen-Chaignon, Vincent Chaptal, Anne Galinier, Grégory Boël, Alain Mazé, Josef Deutscher
HPr kinase/phosphorylase, a Walker motif A-containing bifunctional sensor enzyme controlling catabolite repression in Gram-positive bacteria.
Biochim Biophys Acta: 2004, 1697(1-2);123-35
[PubMed:15023355] [WorldCat.org] [DOI] (P p)

Sylvie Nessler, Sonia Fieulaine, Sandrine Poncet, Anne Galinier, Josef Deutscher, Joël Janin
HPr kinase/phosphorylase, the sensor enzyme of catabolite repression in Gram-positive bacteria: structural aspects of the enzyme and the complex with its protein substrate.
J Bacteriol: 2003, 185(14);4003-10
[PubMed:12837773] [WorldCat.org] [DOI] (P p)


General Analysis, Physiology

Isabelle Gaugué, Jacques Oberto, Harald Putzer, Jacqueline Plumbridge
The use of amino sugars by Bacillus subtilis: presence of a unique operon for the catabolism of glucosamine.
PLoS One: 2013, 8(5);e63025
[PubMed:23667565] [WorldCat.org] [DOI] (I e)

Frederik M Meyer, Matthieu Jules, Felix M P Mehne, Dominique Le Coq, Jens J Landmann, Boris Görke, Stéphane Aymerich, Jörg Stülke
Malate-mediated carbon catabolite repression in Bacillus subtilis involves the HPrK/CcpA pathway.
J Bacteriol: 2011, 193(24);6939-49
[PubMed:22001508] [WorldCat.org] [DOI] (I p)

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)

Holger Ludwig, Nicole Rebhan, Hans-Matti Blencke, Matthias Merzbacher, Jörg Stülke
Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation.
Mol Microbiol: 2002, 45(2);543-53
[PubMed:12123463] [WorldCat.org] [DOI] (P p)

J Reizer, C Hoischen, F Titgemeyer, C Rivolta, R Rabus, J Stülke, D Karamata, M H Saier, W Hillen
A novel protein kinase that controls carbon catabolite repression in bacteria.
Mol Microbiol: 1998, 27(6);1157-69
[PubMed:9570401] [WorldCat.org] [DOI] (P p)

A Galinier, M Kravanja, R Engelmann, W Hengstenberg, M C Kilhoffer, J Deutscher, J Haiech
New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression.
Proc Natl Acad Sci U S A: 1998, 95(4);1823-8
[PubMed:9465101] [WorldCat.org] [DOI] (P p)


Structural Analysis of HPrK


Enzymatic Properties, Mutation Analysis

HprK as a Target For Antimicrobial Compounds

Helena Ramström, Maryline Bourotte, Claude Philippe, Martine Schmitt, Jacques Haiech, Jean-Jacques Bourguignon
Heterocyclic bis-cations as starting hits for design of inhibitors of the bifunctional enzyme histidine-containing protein kinase/phosphatase from Bacillus subtilis.
J Med Chem: 2004, 47(9);2264-75
[PubMed:15084125] [WorldCat.org] [DOI] (P p)