HprK

• Description: HPr kinase/ phosphorylase
  
  

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 Advanced_DNA
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein modification, transcription factors and their control

The gene

Basic information

• Locus tag: BSU35000

Phenotypes of a mutant

no carbon catabolite repression

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:
  • HprK- HPr
  • HprK-Crh PubMed

• Localization:

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)

• UniProt: O34483

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: hprK-lgt-yvoD-yvoE-yvoF PubMed

• Expression browser: hprK PubMed

• Sigma factor:

• 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

• lacZ fusion: pGP201 (in pAC5) available in Stülke lab, pGP202 (in pAC6) 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

References

General Analysis, Physiology

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)