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FeaR DNA-binding transcriptional activator

Synonyms: FeaR
Summary:
Phenylethylamine regulator, FeaR, is considered an activator of phenylacetate synthesis from 2-phenylethylamine (PEA). This regulator is regulated by catabolic repression, and highly expressed in the presence of succinate [3]. FeaR controls expression of a pathway for the degradation of potentially toxic aromatic compounds [2]. It is induced by tyramine, and in the absence of glucose, it activates the expression of amine oxidase and phenylacetaldehyde dehydrogenase, proteins involved in 2-phenylethylamine catabolism [1, 2, 4]. Although it has not been possible to test the ligand binding to FeaR, these data and those of others suggest that it is a substrate or intermediate of the TynA/FeaB pathway, as it is more likely that an aldehyde (tyramine) is the direct inducer for the PEA catabolic pathway and a likely coeffector of FeaR [2].
FeaR belongs to the AraC/XylS family of transcriptional regulators [1, 3].
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Transcription factor      
TF conformation(s):
Name Conformation Type TF-Effector Interaction Type Apo/Holo Conformation Evidence (Confirmed, Strong, Weak) References
FeaR     nd nd
Evolutionary Family: AraC/XylS
Connectivity class: Local Regulator
Gene name: feaR
  Genome position: 1446378-1447283
  Length: 906 bp / 301 aa
Operon name: feaR
TU(s) encoding the TF:
Transcription unit        Promoter
feaR
feaRp
feaR
feaRp1
feaR
feaRp2
feaR
feaRp3


Regulon       
Regulated gene(s) feaB, tynA
Multifun term(s) of regulated gene(s) MultiFun Term (List of genes associated to the multifun term)
amines (2)
nicotinamide adenine dinucleotide (1)
amino acids (1)
threonine catabolism (1)
Regulated operon(s) feaB, tynA
First gene in the operon(s) feaB, tynA
Simple and complex regulons CRP,FeaR,NsrR
FeaR
Simple and complex regulatory phrases Regulatory phrase (List of promoters regulated by the phrase)
[FeaR,+](2)


Transcription factor binding sites (TFBSs) arrangements       

  Functional conformation Function Promoter Sigma factor Central Rel-Pos Distance to first Gene Genes Sequence LeftPos RightPos Evidence (Confirmed, Strong, Weak) References
  FeaR activator feaBp1 Sigma70 -64.0 -91.0 feaB
cgatttgcggAGCTTGTCACAGCTGACAAAGcgaatgtcac
1447418 1447438 [BPP], [GEA], [HIBSCS], [SM] [1], [2]
  FeaR activator feaBp1 Sigma70 -43.0 -70.0 feaB
gctgacaaagCGAATGTCACAGCGAAAAAAGtgacttttct
1447439 1447459 [BPP], [GEA], [HIBSCS], [SM] [2]
  FeaR activator tynAp1 Sigma70 -64.0 -124.0 tynA
actgtatgaaAAGCTGGCACACCTGCCAAACaacctggcag
1451463 1451483 [BPP], [GEA], [HIBSCS], [SM] [2]
  FeaR activator tynAp1 Sigma70 -43.0 -103.0 tynA
cctgccaaacAACCTGGCAGGTGCAGGCAATcccctttgca
1451442 1451462 [BPP], [GEA], [HIBSCS], [SM] [2]


Alignment and PSSM for FeaR TFBSs    

Aligned TFBS of FeaR   
  Sequence
 

Position weight matrix (PWM).   
A	0	0	0	0	3	0	4	0	0	0	1	2	1	4	3	3
C	0	1	1	3	0	4	0	2	4	0	0	2	3	0	0	0
G	1	3	1	0	1	0	0	2	0	1	3	0	0	0	1	1
T	3	0	2	1	0	0	0	0	0	3	0	0	0	0	0	0

PWM logo   


 


Evolutionary conservation of regulatory elements    
     Note: Evolutionary conservation of regulatory interactions and promoters is limited to gammaproteobacteria.
Promoter-target gene evolutionary conservation


Evidence    

 [BPP] Binding of purified proteins

 [GEA] Gene expression analysis

 [HIBSCS] Human inference based on similarity to consensus sequences

 [SM] Site mutation



Reference(s)    

 [1] Hanlon SP., Hill TK., Flavell MA., Stringfellow JM., Cooper RA., 1997, 2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression., Microbiology. 143 ( Pt 2):513-8

 [2] Zeng J., Spiro S., 2013, Finely tuned regulation of the aromatic amine degradation pathway in Escherichia coli., J Bacteriol. 195(22):5141-50

 [3] Yamashita M., Azakami H., Yokoro N., Roh JH., Suzuki H., Kumagai H., Murooka Y., 1996, maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli., J Bacteriol. 178(10):2941-7

 [4] Steinebach V., Benen JA., Bader R., Postma PW., De Vries S., Duine JA., 1996, Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme., Eur J Biochem. 237(3):584-91



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