Difference between revisions of "HprK"

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* '''Additional information:'''
 
* '''Additional information:'''
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** number of protein molecules per cell (minimal medium with glucose and ammonium): 398 {{PubMed|24696501}}
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** number of protein molecules per cell (complex medium with amino acids, without glucose): 875 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 09:36, 17 April 2014

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:
hprK
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:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 398 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 875 PubMed

Biological materials

  • Expression vector:
    • for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP642, available in Jörg Stülke's lab
    • for expression/ purification of mutant HprK-G158A from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP650, available in Jörg Stülke's lab
    • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP205, available in Jörg Stülke's lab
    • for expression, purification of the N-terminal in E. coli with N-terminal His-tag, in pWH844: pGP218, available in Jörg Stülke's lab
  • GFP fusion:
  • two-hybrid system:

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


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

Vincent Chaptal, Fanny Vincent, Virginie Gueguen-Chaignon, Vicente Monedero, Sandrine Poncet, Josef Deutscher, Sylvie Nessler, Solange Morera
Structural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzyme.
J Biol Chem: 2007, 282(48);34952-7
[PubMed:17878158] [WorldCat.org] [DOI] (P p)

Gregory S Allen, Katrin Steinhauer, Wolfgang Hillen, Jörg Stülke, Richard G Brennan
Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae.
J Mol Biol: 2003, 326(4);1203-17
[PubMed:12589763] [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)

Jose Antonio Márquez, Sonja Hasenbein, Brigitte Koch, Sonia Fieulaine, Sylvie Nessler, Robert B Russell, Wolfgang Hengstenberg, Klaus Scheffzek
Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions.
Proc Natl Acad Sci U S A: 2002, 99(6);3458-63
[PubMed:11904409] [WorldCat.org] [DOI] (P p)


Enzymatic Properties, Mutation Analysis

Frédérique Pompeo, Yohann Granet, Jean-Pierre Lavergne, Christophe Grangeasse, Sylvie Nessler, Jean-Michel Jault, Anne Galinier
Regulation and mutational analysis of the HPr kinase/phosphorylase from Bacillus subtilis.
Biochemistry: 2003, 42(22);6762-71
[PubMed:12779331] [WorldCat.org] [DOI] (P p)

Helena Ramström, Sarah Sanglier, Emmanuelle Leize-Wagner, Claude Philippe, Alain Van Dorsselaer, Jacques Haiech
Properties and regulation of the bifunctional enzyme HPr kinase/phosphatase in Bacillus subtilis.
J Biol Chem: 2003, 278(2);1174-85
[PubMed:12411438] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Sandrine Poncet, Anne Galinier, Vicente Monedero, Sonia Fieulaine, Joël Janin, Sylvie Nessler, José Antonio Marquez, Klaus Scheffzek, Sonja Hasenbein, Wolfgang Hengstenberg, Josef Deutscher
Pyrophosphate-producing protein dephosphorylation by HPr kinase/phosphorylase: a relic of early life?
Proc Natl Acad Sci U S A: 2002, 99(21);13442-7
[PubMed:12359880] [WorldCat.org] [DOI] (P p)

K G Hanson, Katrin Steinhauer, Jonathan Reizer, Wolfgang Hillen, Jörg Stülke
HPr kinase/phosphatase of Bacillus subtilis: expression of the gene and effects of mutations on enzyme activity, growth and carbon catabolite repression.
Microbiology (Reading): 2002, 148(Pt 6);1805-1811
[PubMed:12055300] [WorldCat.org] [DOI] (P p)

Jean-Pierre Lavergne, Jean-Michel Jault, Anne Galinier
Insights into the functioning of Bacillus subtilis HPr kinase/phosphatase: affinity for its protein substrates and role of cations and phosphate.
Biochemistry: 2002, 41(20);6218-25
[PubMed:12009882] [WorldCat.org] [DOI] (P p)

Anne Galinier, Jean-Pierre Lavergne, Christophe Geourjon, Sonia Fieulaine, Sylvie Nessler, Jean-Michel Jault
A new family of phosphotransferases with a P-loop motif.
J Biol Chem: 2002, 277(13);11362-7
[PubMed:11796714] [WorldCat.org] [DOI] (P p)

V Monedero, S Poncet, I Mijakovic, S Fieulaine, V Dossonnet, I Martin-Verstraete, S Nessler, J Deutscher
Mutations lowering the phosphatase activity of HPr kinase/phosphatase switch off carbon metabolism.
EMBO J: 2001, 20(15);3928-37
[PubMed:11483496] [WorldCat.org] [DOI] (P p)

J M Jault, S Fieulaine, S Nessler, P Gonzalo, A Di Pietro, J Deutscher, A Galinier
The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding.
J Biol Chem: 2000, 275(3);1773-80
[PubMed:10636874] [WorldCat.org] [DOI] (P p)

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)

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