Difference between revisions of "CcpA"
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=Labs working on this gene/protein= | =Labs working on this gene/protein= | ||
− | + | ** [[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] |
− | + | ** [[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] | + | ** [[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 |
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− | [[Yasutaro Fujita]], University of Fukuyama, Japan | ||
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− | [[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage] | ||
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− | [[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= | ||
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==Reviews== | ==Reviews== | ||
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<pubmed> 8598282 , 19202299,14665673,18628769 ,18359269, 18628769 </pubmed> | <pubmed> 8598282 , 19202299,14665673,18628769 ,18359269, 18628769 </pubmed> | ||
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==General and physiological studies== | ==General and physiological studies== | ||
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<pubmed>1904524 ,10941796 ,12123463,8000527, 18757537,16547058,14523131 </pubmed> | <pubmed>1904524 ,10941796 ,12123463,8000527, 18757537,16547058,14523131 </pubmed> | ||
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==Global analyses (proteome, transcriptome)== | ==Global analyses (proteome, transcriptome)== | ||
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<pubmed>12850135 ,11251851,10559165, 11160890,17183215 </pubmed> | <pubmed>12850135 ,11251851,10559165, 11160890,17183215 </pubmed> | ||
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==Repression of target genes by CcpA== | ==Repression of target genes by CcpA== | ||
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<pubmed>15150224 ,16166551 ,11929549 , 7913927 ,17827291 ,11985717 ,12100558,7592486 </pubmed> | <pubmed>15150224 ,16166551 ,11929549 , 7913927 ,17827291 ,11985717 ,12100558,7592486 </pubmed> | ||
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==Positive regulation of gene expression by CcpA== | ==Positive regulation of gene expression by CcpA== | ||
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<pubmed>8226682 ,12193635 ,10559153 ,15916605, 9811655 ,10986270 </pubmed> | <pubmed>8226682 ,12193635 ,10559153 ,15916605, 9811655 ,10986270 </pubmed> | ||
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==Control of CcpA activity== | ==Control of CcpA activity== | ||
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<pubmed>7623661 ,9973552 ,9334231 ,12051938, 9689125 </pubmed> | <pubmed>7623661 ,9973552 ,9334231 ,12051938, 9689125 </pubmed> | ||
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==CcpA-DNA interaction== | ==CcpA-DNA interaction== | ||
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<pubmed>8596444 ,10666464 ,15885105,7665492 ,9254709 </pubmed> | <pubmed>8596444 ,10666464 ,15885105,7665492 ,9254709 </pubmed> | ||
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==Functional analysis of CcpA== | ==Functional analysis of CcpA== | ||
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<pubmed>10383986 ,10601226 ,11557150,9252590 ,9988473 </pubmed> | <pubmed>10383986 ,10601226 ,11557150,9252590 ,9988473 </pubmed> | ||
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==Structural analyses== | ==Structural analyses== | ||
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<pubmed>15369672 ,16316990 ,17376479 </pubmed> | <pubmed>15369672 ,16316990 ,17376479 </pubmed> | ||
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[[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 ![]() This image was kindly provided by SubtiList
|
Contents
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)
- Protein family: LacI family
- Paralogous protein(s):
Genes controlled by CcpA
- Repression by CcpA: abbA, amyE, bglP-bglH, bglS, cccA, citZ-icd-mdh, levD-levE-levF-levG-sacC, licB-licC-licA-licH, phoP-phoR, xylA-xylB, xynP-xynB
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
- UniProt: P25144
- 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
- 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
- Wolfgang Hillen, Erlangen University, Germany Homepage
- Richard Brennan, Houston, Texas, USA Homepage
- Milton H. Saier, University of California at San Diego, USA Homepage
- Yasutaro Fujita, University of Fukuyama, Japan
- Jörg Stülke, University of Göttingen, Germany Homepage
- Oscar Kuipers, University of Groningen, The Netherlands
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