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 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:

• 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)