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 |
| − | |||
| − | [[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 21:17, 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
Yasutaro Fujita
Carbon catabolite control of the metabolic network in Bacillus subtilis.
Biosci Biotechnol Biochem: 2009, 73(2);245-59
[PubMed:19202299]
[WorldCat.org]
[DOI]
(I p)
Boris Görke, Jörg Stülke
Carbon catabolite repression in bacteria: many ways to make the most out of nutrients.
Nat Rev Microbiol: 2008, 6(8);613-24
[PubMed:18628769]
[WorldCat.org]
[DOI]
(I p)
Josef Deutscher
The mechanisms of carbon catabolite repression in bacteria.
Curr Opin Microbiol: 2008, 11(2);87-93
[PubMed:18359269]
[WorldCat.org]
[DOI]
(P p)
Jessica B Warner, Juke S Lolkema
CcpA-dependent carbon catabolite repression in bacteria.
Microbiol Mol Biol Rev: 2003, 67(4);475-90
[PubMed:14665673]
[WorldCat.org]
[DOI]
(P p)
T M Henkin
The role of CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis.
FEMS Microbiol Lett: 1996, 135(1);9-15
[PubMed:8598282]
[WorldCat.org]
[DOI]
(P p)
General and physiological studies
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
