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
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	34 kDa, 4.906
Gene length, protein length	930 bp, 310 aa
Immediate neighbours	lgt, nagA
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: 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:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: GP202 (spc), GP858 (aphA3), both 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

Reviews

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)

Structural Analysis of HPrK

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)