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 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
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