ccpA
168
Carbon catabolite control protein A, involved in glucose regulation of many genes; represses catabolic genes and activates genes involved in excretion of excess carbon
locus
BSU_29740
Molecular weight
36.78 kDa
pI
5.06
function
carbon catabolite repression (CCR)
product
transcriptional regulator ([wiki|LacI family])
essential
no
synonyms
ccpA, graR, alsA, amyR
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG1609 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
3,044,165 → 3,045,169
Phenotypes of a mutant
Loss of carbon catabolite repression. Loss of [protein|14ED1AF5038F43F3B151FCBABE6CFC5A2DA3AA6E|ptsI]-dependent sugar transport due to excessive phosphorylation of [protein|29B793660E4D30C0656248F3EF403FEF76FB9025|HPr] by [protein|771F205F818A755A661B8E1C95365A4F6AEB05C7|hprK]
The mutant is unable to grow on a minimal medium with glucose and ammonium as the only sources of carbon and nitrogen, respectively, this can be suppressed by mutations resulting in hyperactive [protein|41199C76DF8CA804B7B8878D61228B9542A96AE4|topoisomerase I] or in the inactivation of [gene|56CBEBCFEF5CFB4A0175498338C7AF2F45EAA3E3|rocG] [pubmed|29242163,17183217]
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The protein
Catalyzed reaction/ biological activity
transcriptional regulator of carbon catabolite repression (CCR)
Protein family
[wiki|LacI family]
[wiki|Domains]
[wiki|HTH lacI-type domain] (aa 1-58) (according to UniProt)
DNA binding Domain (6 – 25)
[wiki|Cofactors]
[protein|29B793660E4D30C0656248F3EF403FEF76FB9025|HPr]-Ser46-P, [protein|A269774F2FDC94F93BA5F1360FFFE754B50383AD|crh]-Ser-46-P
Structure
[PDB|3OQM] (complex of ''B. subtilis'' CcpA with P-Ser-[protein|29B793660E4D30C0656248F3EF403FEF76FB9025|HPr] and the ''[gene|DAA285C86692E8B47D48652E0973AE3FF091CBC3|ackA]'' operator site)
[PDB|3OQN] (complex of ''B. subtilis'' CcpA with P-Ser-[protein|29B793660E4D30C0656248F3EF403FEF76FB9025|HPr] and the ''[gene|1C566E54F8EF1A17A365FC49DFDA452AC5D0CA64|gntR]'' operator site)
[PDB|3OQO] (complex of ''B. subtilis'' CcpA with P-Ser-[protein|29B793660E4D30C0656248F3EF403FEF76FB9025|HPr] and a optimal synthetic operator site)
[PDB|2HSG] (apoprotein) [pubmed|17500051]
CcpA-[protein|A269774F2FDC94F93BA5F1360FFFE754B50383AD|crh]-DNA-complex [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=52326 NCBI]
complex with P-Ser-[protein|29B793660E4D30C0656248F3EF403FEF76FB9025|HPr] and sulphate ions [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=39857 NCBI]
[AF|P25144]
Effectors of protein activity
glucose-6-phosphate, fructose-1,6-bisphosphate [Pubmed|17376479]
Expression and Regulation
Operons
genes
[gene|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|ccpA]-[gene|3D42584D65D80A1C73F057714647E29FF6BBD58A|motP]-[gene|6617D785D08C5919F0B774D2AF9EA6A84215486B|motS]
description
[Pubmed|16547058]
regulation
constitutive
sigma factors
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA]: sigma factor, in [regulon|protein:360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA regulon]
additional information
there are about 3.000 molecules of CcpA per cell [http://www.ncbi.nlm.nih.gov/sites/entrez/8000527 PubMed], this corresponds to a concentration of 3 µM (according to [PubMed|20408793])
Biological materials
Mutant
QB5407 (ccpA::spc) [Pubmed|10941796], available in [wiki|Jörg Stülke]'s lab
GP302 (erm) [Pubmed|12123463], available in [wiki|Jörg Stülke]'s lab
GP300 (an in frame deletion of ''[gene|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|ccpA]'') [Pubmed|11557150], available in [wiki|Jörg Stülke]'s lab
WH649 (aphA3), available in [wiki|Gerald Seidel]'s lab
BKE29740 (Δ[gene|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|ccpA]::erm trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKE29740 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATCCTAAAACCACTCCTTT, downstream forward: _UP4_TAAGAAAAACAAAGAGCAAG
BKK29740 (Δ[gene|E39AFEB7B7F28969A35C4B51CC6E7819F71C79D9|ccpA]::kan trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKK29740 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATCCTAAAACCACTCCTTT, downstream forward: _UP4_TAAGAAAAACAAAGAGCAAG
Expression vectors
pGP643 (N-terminal Strep-tag, purification from ''B. subtilis'', for [wiki|SPINE], in [wiki|pGP380]), available in [wiki|Jörg Stülke]'s lab
pWH940 (C-terminal Strep-tag, purification from ''B. subtilis'', for [wiki|SPINE], in [wiki|pGP382]), available in [wiki|Gerald Seidel]'s lab
Antibody
available in [wiki|Gerald Seidel]'s and in [wiki|Jörg Stülke]'s lab
labs
[wiki|Gerald Seidel], Erlangen University, Germany [http://www.biologie.uni-erlangen.de/mibi/index2.html Homepage]
[wiki|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]
[wiki|Milton H. Saier], University of California at San Diego, USA [http://biology.ucsd.edu/faculty/saier.html Homepage]
[wiki|Yasutaro Fujita], University of Fukuyama, Japan
[wiki|Jörg Stülke], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
[wiki|Oscar Kuipers], University of Groningen, The Netherlands [http://molgen.biol.rug.nl/molgen/index.php Homepage]
References
Reviews
Structural analyses
CcpA-DNA interaction
Control of CcpA activity
Functional analysis of CcpA
General and physiological studies
Repression of target genes by CcpA
Positive regulation of gene expression by CcpA
Global analyses (proteome, transcriptome, ChIP-chip)
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Time of last update: 2024-11-28 11:47:22
Author of last update: Jstuelk