Difference between revisions of "Pgk"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
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* no growth on LB medium, the mutant requires glucose and malate for growth
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* essential {{PubMed|12682299}}, non-essential according to {{PubMed|23420519}}   
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* essential according to Kobayashi et al.  [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
 
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pgk_3480197_3481381_-1 pgk] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=pgk_3480197_3481381_-1 pgk] {{PubMed|22383849}}
  
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* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
 
** ''[[cggR]]'': [[SigA]] {{PubMed|11489127}}  
 
** ''[[cggR]]'': [[SigA]] {{PubMed|11489127}}  
 
** ''[[pgk]]'': [[SigA]] {{PubMed|11489127}}  
 
** ''[[pgk]]'': [[SigA]] {{PubMed|11489127}}  
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=References=
 
=References=
  
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<pubmed> 16479537, 12850135 , 17726680, 11489127 ,17505547 , 17218307 7154941 12682299 </pubmed>
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<pubmed> 16479537, 12850135 , 17726680, 11489127 ,17505547 , 17218307 7154941 12682299 23420519</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:36, 14 April 2013

Gene name pgk
Synonyms
Essential No
Product phosphoglycerate kinase
Function enzyme in glycolysis/ gluconeogenesis
Gene expression levels in SubtiExpress: pgk
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 42,0 kDa, 4.77
Gene length, protein length 1182 bp, 394 amino acids
Immediate neighbours tpi, gapA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Pgk context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Pgk expression.png















Categories containing this gene/protein

ATP synthesis, carbon core metabolism, phosphoproteins, universally conserved proteins

This gene is a member of the following regulons

CggR regulon

The gene

Basic information

  • Locus tag: BSU33930

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + 3-phospho-D-glycerate = ADP + 1,3-bisphosphoglycerate (according to Swiss-Prot)
  • Protein family: phosphoglycerate kinase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Two Substrate Reversible Michaelis-Menten PubMed
  • Domains:
    • nucleotide binding domain (ATP) (350–353)
    • 2x substrate binding domain (21–23), (59–62)
  • Modification: phosphorylation on Ser-183 AND Thr-299 PubMed, PubMed
  • Cofactor(s): Mg2+ or Mn2+ PubMed
  • Effectors of protein activity:
    • Inhibited by Co2+, NDP and NMP PubMed

Database entries

  • Structure: 1PHP (from Geobacillus stearothermophilus)
  • KEGG entry: [3]

Additional information

  • extensive information on the structure and enzymatic properties of Pgk can be found at Proteopedia

Expression and regulation

  • Regulatory mechanism: transcription repression by CggR PubMed
  • Additional information:

Biological materials

  • Mutant:
    • GP699 (pgk::cat), available in Stülke lab
    • GP707 (pgk::erm), available in Stülke lab
  • Expression vector:
    • pGP1102 (N-terminal His-tag, in pWH844), available in Stülke lab
    • pGP95 (N-terminal Strep-tag, in pGP172), available in Stülke lab
    • pGP91 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
    • pGP1513 (expression in B. subtilis, in pBQ200), available in Stülke lab
  • lacZ fusion: pGP514 (in pAC6), a series of promoter deletion variants is also available in pAC6, available in Stülke lab
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Fabian M Commichau, Nico Pietack, Jörg Stülke
Essential genes in Bacillus subtilis: a re-evaluation after ten years.
Mol Biosyst: 2013, 9(6);1068-75
[PubMed:23420519] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Laurent Jannière, Danielle Canceill, Catherine Suski, Sophie Kanga, Bérengère Dalmais, Roxane Lestini, Anne-Françoise Monnier, Jérôme Chapuis, Alexander Bolotin, Marina Titok, Emmanuelle Le Chatelier, S Dusko Ehrlich
Genetic evidence for a link between glycolysis and DNA replication.
PLoS One: 2007, 2(5);e447
[PubMed:17505547] [WorldCat.org] [DOI] (I e)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

K Kobayashi, S D Ehrlich, A Albertini, G Amati, K K Andersen, M Arnaud, K Asai, S Ashikaga, S Aymerich, P Bessieres, F Boland, S C Brignell, S Bron, K Bunai, J Chapuis, L C Christiansen, A Danchin, M Débarbouille, E Dervyn, E Deuerling, K Devine, S K Devine, O Dreesen, J Errington, S Fillinger, S J Foster, Y Fujita, A Galizzi, R Gardan, C Eschevins, T Fukushima, K Haga, C R Harwood, M Hecker, D Hosoya, M F Hullo, H Kakeshita, D Karamata, Y Kasahara, F Kawamura, K Koga, P Koski, R Kuwana, D Imamura, M Ishimaru, S Ishikawa, I Ishio, D Le Coq, A Masson, C Mauël, R Meima, R P Mellado, A Moir, S Moriya, E Nagakawa, H Nanamiya, S Nakai, P Nygaard, M Ogura, T Ohanan, M O'Reilly, M O'Rourke, Z Pragai, H M Pooley, G Rapoport, J P Rawlins, L A Rivas, C Rivolta, A Sadaie, Y Sadaie, M Sarvas, T Sato, H H Saxild, E Scanlan, W Schumann, J F M L Seegers, J Sekiguchi, A Sekowska, S J Séror, M Simon, P Stragier, R Studer, H Takamatsu, T Tanaka, M Takeuchi, H B Thomaides, V Vagner, J M van Dijl, K Watabe, A Wipat, H Yamamoto, M Yamamoto, Y Yamamoto, K Yamane, K Yata, K Yoshida, H Yoshikawa, U Zuber, N Ogasawara
Essential Bacillus subtilis genes.
Proc Natl Acad Sci U S A: 2003, 100(8);4678-83
[PubMed:12682299] [WorldCat.org] [DOI] (P p)

H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol Microbiol: 2001, 41(2);409-22
[PubMed:11489127] [WorldCat.org] [DOI] (P p)

K Suzuki, K Imahori
Phosphoglycerate kinase from Bacillus stearothermophilus.
Methods Enzymol: 1982, 90 Pt E;126-30
[PubMed:7154941] [WorldCat.org] [DOI] (P p)

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