RegulonDB RegulonDB 10.9: Gene Form
   

fecR gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

fecA fecR fecI ykiE SlyA Fur Fur Fur Fur Fur Fur Fur PdhR insAp14 insAp14 TSS_5124 TSS_5124 fecIp fecIp fecAp fecAp

Gene      
Name: fecR    Texpresso search in the literature
Synonym(s): ECK4282, EG10292, b4292
Genome position(nucleotides): 4516764 <-- 4517717 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 59.01
External database links:  
ASAP:
 ABE-0014070
CGSC:
 35627
ECHOBASE:
 EB0288
ECOLIHUB:
 fecR
OU-MICROARRAY:
 b4292
STRING:
 511145.b4292
COLOMBOS: fecR


Shine dalgarno      
Sequence: ctgttccgtcTGGAGTatgggtTAT


Product      
Name: ferric citrate regulator FecR
Synonym(s): FecR, anti-sigma factor FecR
Sequence: Get amino acid sequence Fasta Format
Cellular location: periplasmic space,inner membrane
Molecular weight: 35.532
Isoelectric point: 9.37
Motif(s):
 
Type Positions Sequence
50 -> 50 W
15 -> 56 SASHWYAVLSGERVSPQQEARWQQWYEQDQDNQWAWQQVENL
39 -> 39 W
127 -> 127 S
13 -> 13 L

 
Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.2 - RNA related --> 2.2.2 - Transcription related
  3 - regulation --> 3.1 - type of regulation --> 3.1.2 - transcriptional level --> 3.1.2.4 - complex regulation
  5 - cell processes --> 5.5 - adaptations --> 5.5.7 - Fe aquisition
Gene Ontology Terms (GO)  
cellular_component GO:0042597 - periplasmic space
GO:0005887 - integral component of plasma membrane
molecular_function GO:0005515 - protein binding
GO:0016989 - sigma factor antagonist activity
GO:0004888 - transmembrane signaling receptor activity
biological_process GO:0023019 - signal transduction involved in regulation of gene expression
GO:0006811 - ion transport
GO:0050896 - response to stimulus
GO:0006879 - cellular iron ion homeostasis
GO:0055072 - iron ion homeostasis
GO:2000142 - regulation of DNA-templated transcription, initiation
GO:1903507 - negative regulation of nucleic acid-templated transcription
Note(s): Note(s): ...[more].
Evidence: [IMP] Inferred from mutant phenotype
Reference(s): [1] Angerer A., et al., 1998
[2] Angerer A., et al., 1995
[3] Breidenstein E., et al., 2006
[4] Brooks BE., et al., 2008
[5] Enz S., et al., 2003
[6] Mahren S., et al., 2005
[7] Ochs M., et al., 1995
[8] Van Hove B., et al., 1990
[9] Wriedt K., et al., 1995
External database links:  
DIP:
 DIP-9589N
ECOCYC:
 EG10292-MONOMER
ECOLIWIKI:
 b4292
INTERPRO:
 IPR032623
INTERPRO:
 IPR012373
INTERPRO:
 IPR006860
PANTHER:
 PTHR30273
PFAM:
 PF04773
PFAM:
 PF16220
PRIDE:
 P23485
PRODB:
 PRO_000022596
REFSEQ:
 NP_418712
SMR:
 P23485
UNIPROT:
 P23485


Operon      
Name: fecIR         
Operon arrangement:
Transcription unit        Promoter
fecIR


Transcriptional Regulation      
Display Regulation             
Repressed by: SlyA, Fur


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_5124 4518374 forward nd [RS-EPT-CBR] [10]
  promoter insAp14 4518379 forward Similarity to the consensus
Read more > 		[ICWHO] [11]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

 [ICWHO] Inferred computationally without human oversight


Reference(s)    

 [1] Angerer A., Braun V., 1998, Iron regulates transcription of the Escherichia coli ferric citrate transport genes directly and through the transcription initiation proteins., Arch Microbiol 169(6):483-90

 [2] Angerer A., Enz S., Ochs M., Braun V., 1995, Transcriptional regulation of ferric citrate transport in Escherichia coli K-12. Fecl belongs to a new subfamily of sigma 70-type factors that respond to extracytoplasmic stimuli., Mol Microbiol 18(1):163-74

 [3] Breidenstein E., Mahren S., Braun V., 2006, Residues involved in FecR binding are localized on one side of the FecA signaling domain in Escherichia coli., J Bacteriol 188(17):6440-2

 [4] Brooks BE., Buchanan SK., 2008, Signaling mechanisms for activation of extracytoplasmic function (ECF) sigma factors., Biochim Biophys Acta 1778(9):1930-45

 [5] Enz S., Brand H., Orellana C., Mahren S., Braun V., 2003, Sites of interaction between the FecA and FecR signal transduction proteins of ferric citrate transport in Escherichia coli K-12., J Bacteriol 185(13):3745-52

 [6] Mahren S., Schnell H., Braun V., 2005, Occurrence and regulation of the ferric citrate transport system in Escherichia coli B, Klebsiella pneumoniae, Enterobacter aerogenes, and Photorhabdus luminescens., Arch Microbiol 184(3):175-86

 [7] Ochs M., Veitinger S., Kim I., Welz D., Angerer A., Braun V., 1995, Regulation of citrate-dependent iron transport of Escherichia coli: fecR is required for transcription activation by FecI., Mol Microbiol 15(1):119-32

 [8] Van Hove B., Staudenmaier H., Braun V., 1990, Novel two-component transmembrane transcription control: regulation of iron dicitrate transport in Escherichia coli K-12., J Bacteriol 172(12):6749-58

 [9] Wriedt K., Angerer A., Braun V., 1995, Transcriptional regulation from the cell surface: conformational changes in the transmembrane protein FecR lead to altered transcription of the ferric citrate transport genes in Escherichia coli., J Bacteriol 177(11):3320-2

 [10] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

 [11] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

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