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

• BsubCyc: BSU35000

• 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

• BsubCyc: BSU35000

• 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) PubMed, all available in Jörg Stülke's lab

• 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

• lacZ fusion: pGP201 (in pAC5, PubMed) available in Stülke lab, pGP202 (in pAC6, PubMed) available in Jörg Stülke's lab

• GFP fusion:

• two-hybrid system:

• Antibody: available in Jörg Stülke's lab PubMed

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

Boris Görke, Jörg Stülke
Carbon catabolite repression in bacteria: many ways to make the most out of nutrients.
Nat Rev Microbiol: 2008, 6(8);613-24
[PubMed:18628769] [WorldCat.org] [DOI] (I p)

Sandrine Poncet, Ivan Mijakovic, Sylvie Nessler, Virginie Gueguen-Chaignon, Vincent Chaptal, Anne Galinier, Grégory Boël, Alain Mazé, Josef Deutscher
HPr kinase/phosphorylase, a Walker motif A-containing bifunctional sensor enzyme controlling catabolite repression in Gram-positive bacteria.
Biochim Biophys Acta: 2004, 1697(1-2);123-35
[PubMed:15023355] [WorldCat.org] [DOI] (P p)

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

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)

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)