Difference between revisions of "FapR"
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|style="background:#ABCDEF;" align="center"|'''Function''' || regulation of fatty acid biosynthesis | |style="background:#ABCDEF;" align="center"|'''Function''' || regulation of fatty acid biosynthesis | ||
|- | |- | ||
− | |colspan="2" style="background:#FAF8CC;" align="center"| ''' | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU15880 fapR] |
|- | |- | ||
− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/ | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=FapR FapR] |
+ | |- | ||
+ | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=fapR fapR]''' | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 5.393 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 5.393 | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[recG]]'', ''[[plsX]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[recG]]'', ''[[plsX]]'' | ||
|- | |- | ||
− | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU15880 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU15880 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU15880 DNA_with_flanks] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:ylpC_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:ylpC_context.gif]] | ||
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
+ | |- | ||
+ | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=fapR_1661967_1662533_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:fapR_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU15880]] | ||
|- | |- | ||
|} | |} | ||
__TOC__ | __TOC__ | ||
− | + | <br/><br/><br/><br/> | |
− | <br/><br/><br/><br/><br/><br/> | + | <br/><br/><br/><br/> |
+ | <br/><br/><br/><br/> | ||
+ | <br/><br/> | ||
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15880&redirect=T BSU15880] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/fapR-plsX-fabDG.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/fapR-plsX-fabDG.html] | ||
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* '''Effectors of protein activity:''' malonyl-CoA and malonyl-[[AcpA|ACP]] act as the molecular inducer of the FapR regulon {{PubMed|20201588}} | * '''Effectors of protein activity:''' malonyl-CoA and malonyl-[[AcpA|ACP]] act as the molecular inducer of the FapR regulon {{PubMed|20201588}} | ||
− | * '''Interactions:''' malonyl-[[AcpA|ACP]]-[[FapR]] {{PubMed|20201588}} | + | * '''[[SubtInteract|Interactions]]:''' |
+ | ** malonyl-[[AcpA|ACP]]-[[FapR]] {{PubMed|20201588}} | ||
− | * '''Localization:''' | + | * '''[[Localization]]:''' |
=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15880&redirect=T BSU15880] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2F3X 2F3X] (complex with effector), [http://www.rcsb.org/pdb/explore.do?structureId=2F41 2F41] | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2F3X 2F3X] (complex with effector), [http://www.rcsb.org/pdb/explore.do?structureId=2F41 2F41] | ||
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* '''Operon:''' ''[[fapR]]-[[plsX]]-[[fabD]]-[[fabG]]-[[acpA]]'' {{PubMed|12737802,19850612}} | * '''Operon:''' ''[[fapR]]-[[plsX]]-[[fabD]]-[[fabG]]-[[acpA]]'' {{PubMed|12737802,19850612}} | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=fapR_1661967_1662533_1 fapR] {{PubMed|22383849}} |
+ | |||
+ | * '''Sigma factor:''' [[SigA]] {{PubMed|16932747}} | ||
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 85 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 490 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 412 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 729 {{PubMed|21395229}} | ||
=Biological materials = | =Biological materials = | ||
− | |||
* '''Mutant:''' | * '''Mutant:''' | ||
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<pubmed>12737802, </pubmed> | <pubmed>12737802, </pubmed> | ||
==Other original publications== | ==Other original publications== | ||
− | <pubmed>18941141, 18820022, 18384517, 16932747,19850612 16091051 20201588</pubmed> | + | '''Additional publications:''' {{PubMed|23102226}} |
+ | <pubmed>18941141, 18820022, 18384517, 16932747,19850612 16091051 20201588 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Latest revision as of 14:19, 17 April 2014
- Description: repressor of fatty acid synthetic genes
Gene name | fapR |
Synonyms | ylpC |
Essential | no |
Product | transcriptional repressor |
Function | regulation of fatty acid biosynthesis |
Gene expression levels in SubtiExpress: fapR | |
Interactions involving this protein in SubtInteract: FapR | |
Metabolic function and regulation of this protein in SubtiPathways: fapR | |
MW, pI | 21 kDa, 5.393 |
Gene length, protein length | 564 bp, 188 aa |
Immediate neighbours | recG, plsX |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biosynthesis of lipids, transcription factors and their control
This gene is a member of the following regulons
The FapR regulon
The gene
Basic information
- Locus tag: BSU15880
Phenotypes of a mutant
Database entries
- BsubCyc: BSU15880
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: FapR regulates the expression of at least 10 genes (the fap regulon). It autoregulates its own expression. Malonyl-CoA, a precursor of fatty acid biosynthesis, binds to FapR changing its conformation to a non-DNA binding state. Hence, conditions that cause malonyl-CoA accumulation, like fatty acid biosynthesis inhibition, derepress the fap regulon.
- Protein family: fapR family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: malonyl-CoA and malonyl-ACP act as the molecular inducer of the FapR regulon PubMed
Database entries
- BsubCyc: BSU15880
- UniProt: O34835
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 85 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 490 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 412 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 729 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
The FapR regulon
Other original publications
Additional publications: PubMed