Difference between revisions of "Pgk"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 12006 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 12006 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 10462 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 10462 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 5859 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2120 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2593 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''  
 
* '''Mutant:'''  
 
** GP699 (''pgk''::''cat''), available in [[Jörg Stülke]]'s lab, {{PubMed|23420519}}lab
 
** GP699 (''pgk''::''cat''), available in [[Jörg Stülke]]'s lab, {{PubMed|23420519}}lab

Revision as of 14:11, 17 April 2014

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:
pgk
MW, pI 42,0 kDa, 4.77
Gene length, protein length 1182 bp, 394 amino acids
Immediate neighbours tpi, gapA
Sequences Protein DNA DNA_with_flanks
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, most abundant 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
  • 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:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 12006 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 10462 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 5859 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2120 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2593 PubMed

Biological materials

  • lacZ fusion: pGP514 (in pAC6), a series of promoter deletion variants is also available in pAC6, available in Jörg Stülke's lab
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available iin Jörg Stülke's 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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)