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: 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 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: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

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

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)