Difference between revisions of "AckA"

From SubtiWiki
Jump to: navigation, search
m (Reverted edits by 134.76.70.252 (talk) to last revision by 134.76.38.147)
Line 122: Line 122:
 
* '''Additional information:'''
 
* '''Additional information:'''
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
** number of protein molecules per cell (minimal medium with glucose and ammonium): 1613 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 11040 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1758 {{PubMed|21395229}}
 
  
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2419 {{PubMed|21395229}}
+
=Biological materials =
  
=Biological materials =
 
 
* '''Mutant:'''  
 
* '''Mutant:'''  
  

Revision as of 13:42, 17 April 2014

  • Description: acetate kinase

Gene name ackA
Synonyms
Essential no
Product acetate kinase
Function overflow metabolism
Gene expression levels in SubtiExpress: ackA
Metabolic function and regulation of this protein in SubtiPathways:
ackA
MW, pI 42 kDa, 5.191
Gene length, protein length 1185 bp, 395 aa
Immediate neighbours moaB, ytxK
Sequences Protein DNA DNA_with_flanks
Genetic context
AckA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AckA expression.png
















Categories containing this gene/protein

ATP synthesis, carbon core metabolism, most abundant proteins

This gene is a member of the following regulons

CcpA regulon, CodY regulon

The gene

Basic information

  • Locus tag: BSU29470

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + acetate = ADP + acetyl phosphate (according to Swiss-Prot)
  • Protein family: acetokinase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 2IIR (from Thermotoga maritima, 54% identity, 73% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expression activated by glucose (2.5 fold) (CcpA) PubMed
    • activated during growth in the presence of branched chain amino acids (CodY) PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Linc Sonenshein, Tufts University, Boston, MA, USA Homepage

Your additional remarks

References

Reviews

Cheryl Ingram-Smith, Stephen R Martin, Kerry S Smith
Acetate kinase: not just a bacterial enzyme.
Trends Microbiol: 2006, 14(6);249-53
[PubMed:16678422] [WorldCat.org] [DOI] (P p)

Alan J Wolfe
The acetate switch.
Microbiol Mol Biol Rev: 2005, 69(1);12-50
[PubMed:15755952] [WorldCat.org] [DOI] (P p)

Original publications

Maria A Schumacher, Mareen Sprehe, Maike Bartholomae, Wolfgang Hillen, Richard G Brennan
Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-affinity binding to degenerate DNA operators.
Nucleic Acids Res: 2011, 39(7);2931-42
[PubMed:21106498] [WorldCat.org] [DOI] (I p)

Robert P Shivers, Sean S Dineen, Abraham L Sonenshein
Positive regulation of Bacillus subtilis ackA by CodY and CcpA: establishing a potential hierarchy in carbon flow.
Mol Microbiol: 2006, 62(3);811-22
[PubMed:16995897] [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)

T R Moir-Blais, F J Grundy, T M Henkin
Transcriptional activation of the Bacillus subtilis ackA promoter requires sequences upstream of the CcpA binding site.
J Bacteriol: 2001, 183(7);2389-93
[PubMed:11244084] [WorldCat.org] [DOI] (P p)

A J Turinsky, F J Grundy, J H Kim, G H Chambliss, T M Henkin
Transcriptional activation of the Bacillus subtilis ackA gene requires sequences upstream of the promoter.
J Bacteriol: 1998, 180(22);5961-7
[PubMed:9811655] [WorldCat.org] [DOI] (P p)

F J Grundy, D A Waters, S H Allen, T M Henkin
Regulation of the Bacillus subtilis acetate kinase gene by CcpA.
J Bacteriol: 1993, 175(22);7348-55
[PubMed:8226682] [WorldCat.org] [DOI] (P p)