Difference between revisions of "HprK"

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(Biological materials)
(Biological materials)
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=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' GP202 (spc) {{PubMed|12055300}}, GP858 (aphA3) {{PubMed|18757537}}, GP82 (cat), available in [[Stülke]] lab
+
* '''Mutant:''' GP202 (spc) {{PubMed|12055300}}, GP858 (aphA3) {{PubMed|18757537}}, GP82 (cat) {{PubMed|21992469}}, all available in [[Jörg Stülke]]'s lab
  
 
* '''Expression vector:'''  
 
* '''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 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 [[Stülke]] 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 [[Stülke]] 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 [[Stülke]] 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]]) available in [[Stülke]] lab, pGP202 (in [[pAC6]]) available in [[Stülke]] lab
+
* '''lacZ fusion:''' pGP201 (in [[pAC5]], {{PubMed|12055300}}) available in [[Stülke]] lab, pGP202 (in [[pAC6]], {{PubMed|12055300}}) available in [[Jörg Stülke]]'s lab
  
 
* '''GFP fusion:'''
 
* '''GFP fusion:'''
Line 139: Line 139:
 
* '''two-hybrid system:'''  
 
* '''two-hybrid system:'''  
  
* '''Antibody:''' available in [[Stülke]] lab
+
* '''Antibody:''' available in [[Jörg Stülke]]'s lab {{PubMed|12055300}}
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=

Revision as of 17:09, 16 January 2014

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
HprK context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
HprK expression.png















Categories containing this gene/protein

protein modification, transcription factors and their control

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU35000

Phenotypes of a mutant

no carbon catabolite repression

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

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:

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)
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • 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
  • GFP fusion:
  • two-hybrid system:

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

Your additional remarks

References

Reviews


General Analysis, Physiology


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

HprK as a Target For Antimicrobial Compounds