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
Isoelectric point
5.06
Function
carbon catabolite repression (CCR)
Product
transcriptional regulator (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 PtsI-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, this can be suppressed by mutations resulting in hyperactive Topoisomerase I or in the inactivation of rocG PubMed
The protein
Catalyzed reaction/ biological activity
transcriptional regulator of carbon catabolite repression (CCR)
Protein family
HTH lacI-type domain (aa 1-58) (according to UniProt)
DNA binding Domain (6 – 25)
Structure
3OQO (PDB) (complex of B. subtilis CcpA with P-Ser-HPr and a optimal synthetic operator site)
2HSG (PDB) (apoprotein) PubMed
Effectors of protein activity
glucose-6-phosphate, fructose-1,6-bisphosphate PubMed
Expression and Regulation
Operons
Additional information
Biological materials
Mutant
QB5407 (ccpA::spc) PubMed, available in Jörg Stülke's lab
GP302 (erm) PubMed, available in Jörg Stülke's lab
WH649 (aphA3), available in Gerald Seidel's lab
Expression vectors
pGP643 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Jörg Stülke's lab
pWH940 (C-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP382), available in Gerald Seidel's lab
Antibody
available in Gerald Seidel's and in Jörg Stülke's lab
Labs working on this gene/protein
Gerald Seidel, 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 Homepage
References
Reviews
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Structural analyses
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CcpA-DNA interaction
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Control of CcpA activity
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Functional analysis of CcpA
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General and physiological studies
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Repression of target genes by CcpA
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Positive regulation of gene expression by CcpA
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Global analyses (proteome, transcriptome, ChIP-chip)
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Time of last update: 2025-04-03 19:17:59
Author of last update: Jstuelk