Difference between revisions of "CcpA"

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(References)
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=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
 
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** [[Wolfgang Hillen]], Erlangen University, Germany [http://www.biologie.uni-erlangen.de/mibi/index2.html Homepage]
[[Wolfgang Hillen]], Erlangen University, Germany [http://www.biologie.uni-erlangen.de/mibi/index2.html Homepage]
+
** [[Richard Brennan]], Houston, Texas, USA [http://www.mdanderson.org/departments/biochem/display.cfm?id=556ef368-6c81-4043-b74f350d41dd06cb&method=displayfull&pn=a8427ebd-d0ff-11d4-80fd00508b603a14 Homepage]
 
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** [[Milton H. Saier]], University of California at San Diego, USA [http://biology.ucsd.edu/faculty/saier.html Homepage]
[[Richard Brennan]], Houston, Texas, USA [http://www.mdanderson.org/departments/biochem/display.cfm?id=556ef368-6c81-4043-b74f350d41dd06cb&method=displayfull&pn=a8427ebd-d0ff-11d4-80fd00508b603a14 Homepage]
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** [[Yasutaro Fujita]], University of Fukuyama, Japan
 
+
** [[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
[[Milton H. Saier]], University of California at San Diego, USA [http://biology.ucsd.edu/faculty/saier.html Homepage]
+
** [[Oscar Kuipers]], University of Groningen, The Netherlands
 
 
[[Yasutaro Fujita]], University of Fukuyama, Japan
 
 
 
[[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
 
 
 
[[Oscar Kuipers]], University of Groningen, The Netherlands
 
 
[http://molgen.biol.rug.nl/molgen/index.php Homepage]
 
[http://molgen.biol.rug.nl/molgen/index.php Homepage]
  
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=References=
 
=References=
 
 
==Reviews==
 
==Reviews==
 
 
<pubmed> 8598282 , 19202299,14665673,18628769 ,18359269, 18628769    </pubmed>
 
<pubmed> 8598282 , 19202299,14665673,18628769 ,18359269, 18628769    </pubmed>
 
 
==General and physiological studies==
 
==General and physiological studies==
 
 
<pubmed>1904524 ,10941796 ,12123463,8000527, 18757537,16547058,14523131 </pubmed>
 
<pubmed>1904524 ,10941796 ,12123463,8000527, 18757537,16547058,14523131 </pubmed>
 
 
==Global analyses (proteome, transcriptome)==
 
==Global analyses (proteome, transcriptome)==
 
 
<pubmed>12850135 ,11251851,10559165, 11160890,17183215 </pubmed>
 
<pubmed>12850135 ,11251851,10559165, 11160890,17183215 </pubmed>
 
 
==Repression of target genes by CcpA==
 
==Repression of target genes by CcpA==
 
 
<pubmed>15150224 ,16166551 ,11929549 , 7913927 ,17827291 ,11985717 ,12100558,7592486  </pubmed>
 
<pubmed>15150224 ,16166551 ,11929549 , 7913927 ,17827291 ,11985717 ,12100558,7592486  </pubmed>
 
 
==Positive regulation of gene expression by CcpA==
 
==Positive regulation of gene expression by CcpA==
 
 
<pubmed>8226682 ,12193635 ,10559153 ,15916605, 9811655 ,10986270 </pubmed>
 
<pubmed>8226682 ,12193635 ,10559153 ,15916605, 9811655 ,10986270 </pubmed>
 
 
==Control of CcpA activity==
 
==Control of CcpA activity==
 
 
<pubmed>7623661 ,9973552 ,9334231 ,12051938, 9689125 </pubmed>
 
<pubmed>7623661 ,9973552 ,9334231 ,12051938, 9689125 </pubmed>
 
 
==CcpA-DNA interaction==
 
==CcpA-DNA interaction==
 
 
<pubmed>8596444 ,10666464 ,15885105,7665492 ,9254709  </pubmed>
 
<pubmed>8596444 ,10666464 ,15885105,7665492 ,9254709  </pubmed>
 
 
==Functional analysis of CcpA==
 
==Functional analysis of CcpA==
 
 
<pubmed>10383986 ,10601226 ,11557150,9252590 ,9988473  </pubmed>
 
<pubmed>10383986 ,10601226 ,11557150,9252590 ,9988473  </pubmed>
 
 
==Structural analyses==
 
==Structural analyses==
 
 
<pubmed>15369672 ,16316990 ,17376479 </pubmed>
 
<pubmed>15369672 ,16316990 ,17376479 </pubmed>
 
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 22:17, 15 December 2009

  • Description: Carbon catabolite control protein A, involved in glucose regulation of many genes; represses catabolic genes and activates genes involved in excretion of excess carbon

Gene name ccpA
Synonyms graR, alsA, amyR
Essential no
Product transcriptional regulator (LacI family)
Function mediates carbon catabolite repression (CCR)
Metabolic function and regulation of this protein in SubtiPathways:
Nucleoside catabolism, Nucleotides (regulation), Ile, Leu, Val,
His, Coenzyme A, Central C-metabolism
MW, pI 36,8 kDa, 5.06
Gene length, protein length 1002 bp, 334 amino acids
Immediate neighbours motP, aroA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CcpA context.gif
This image was kindly provided by SubtiList





The gene

Basic information

  • Locus tag: BSU29740

Phenotypes of a mutant

Loss of carbon catabolite repression. Loss of PTS-dependent sugar transport due to excessive phosphorylation of HPr by HprK. The mutant is unable to grow on a minimal medium with glucose and ammonium as the only sources of carbon and nitrogen, respectively.

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transcriptional regulator of carbon catabolite repression (CCR)
  • Paralogous protein(s):

Genes controlled by CcpA

Extended information on the protein

  • Kinetic information:
  • Domains:
    • HTH lacI-type Domain (1 – 58)
    • DNA binding Domain (6 – 25)
  • Modification:
  • Cofactor(s): HPr-Ser46-P, Crh-Ser-46-P
  • Effectors of protein activity:glucose-6-phosphate, fructose-1,6-bisphosphate Pubmed
  • Localization:

Database entries

  • Structure: 2JCG (Apoprotein from Bacillus megaterium), CcpA-Crh-DNA-complex NCBI, complex with P-Ser-HPr and sulphate ions NCBI
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation: constitutively expressed PubMed
  • Additional information: there are about 3.000 molecules of CcpA per cell PubMed

Biological materials

  • Mutant: QB5407 (spc), GP302 (erm), GP300 (an in frame deletion of ccpA), available in Stülke lab
  • Expression vector: pGP643 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab
  • lacZ fusion:
  • GFP fusion:

Labs working on this gene/protein

Homepage

Your additional remarks

References

Reviews

General and physiological studies

Kalpana D Singh, Matthias H Schmalisch, Jörg Stülke, Boris Görke
Carbon catabolite repression in Bacillus subtilis: quantitative analysis of repression exerted by different carbon sources.
J Bacteriol: 2008, 190(21);7275-84
[PubMed:18757537] [WorldCat.org] [DOI] (I p)

Naoya Terahara, Makoto Fujisawa, Benjamin Powers, Tina M Henkin, Terry A Krulwich, Masahiro Ito
An intergenic stem-loop mutation in the Bacillus subtilis ccpA-motPS operon increases motPS transcription and the MotPS contribution to motility.
J Bacteriol: 2006, 188(7);2701-5
[PubMed:16547058] [WorldCat.org] [DOI] (P p)

Ingrid Wacker, Holger Ludwig, Irene Reif, Hans-Matti Blencke, Christian Detsch, Jörg Stülke
The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA.
Microbiology (Reading): 2003, 149(Pt 10);3001-3009
[PubMed:14523131] [WorldCat.org] [DOI] (P p)

Holger Ludwig, Nicole Rebhan, Hans-Matti Blencke, Matthias Merzbacher, Jörg Stülke
Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation.
Mol Microbiol: 2002, 45(2);543-53
[PubMed:12123463] [WorldCat.org] [DOI] (P p)

N Faires, S Tobisch, S Bachem, I Martin-Verstraete, M Hecker, J Stülke
The catabolite control protein CcpA controls ammonium assimilation in Bacillus subtilis.
J Mol Microbiol Biotechnol: 1999, 1(1);141-8
[PubMed:10941796] [WorldCat.org] (P p)

Y Miwa, M Saikawa, Y Fujita
Possible function and some properties of the CcpA protein of Bacillus subtilis.
Microbiology (Reading): 1994, 140 ( Pt 10);2567-75
[PubMed:8000527] [WorldCat.org] [DOI] (P p)

T M Henkin, F J Grundy, W L Nicholson, G H Chambliss
Catabolite repression of alpha-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacl and galR repressors.
Mol Microbiol: 1991, 5(3);575-84
[PubMed:1904524] [WorldCat.org] [DOI] (P p)

Global analyses (proteome, transcriptome)

Repression of target genes by CcpA

Positive regulation of gene expression by CcpA

Control of CcpA activity

CcpA-DNA interaction

Functional analysis of CcpA

Structural analyses