RegulonDB RegulonDB 11.1: Gene Form
   

pheT gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

pheT pheS ihfA IHF IHF IHF TSS_2011 TSS_2011 TSS_2010 TSS_2010 TSS_2009 TSS_2009 TSS_2008 TSS_2008 TSS_2007 TSS_2007 ihfAp4 ihfAp4 TSS_2006 TSS_2006 TSS_2005 TSS_2005 TSS_2004 TSS_2004 TSS_2003 TSS_2003

Gene      
Name: pheT    Texpresso search in the literature
Synonym(s): ECK1711, EG10710, b1713
Genome position(nucleotides): 1795557 <-- 1797944
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 54.36
External database links:  
ASAP:
 ABE-0005717
CGSC:
 399
ECHOBASE:
 EB0704
ECOLIHUB:
 pheT
OU-MICROARRAY:
 b1713
STRING:
 511145.b1713
COLOMBOS: pheT


Product      
Name: phenylalanine—tRNA ligase subunit β
Synonym(s): PheT
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol,membrane
Molecular weight: 87.378
Isoelectric point: 4.94
Motif(s):
 
Type Positions Sequence Comment
39 -> 148 AGSFHGVVVGEVVECAQHPNADKLRVTKVNVGGDRLLDIVCGAPNCRQGLRVAVATIGAVLPGDFKIKAAKLRGEPSEGMLCSFSELGISDDHSGIIELPADAPIGTDIR UniProt: tRNA-binding.
45 -> 145 VVVGEVVECAQHPNADKLRVTKVNVGGDRLLDIVCGAPNCRQGLRVAVATIGAVLPGDFKIKAAKLRGEPSEGMLCSFSELGISDDHSGIIELPADAPIGT
93 -> 93 A UniProt: In Ref. 1; CAA23565..
141 -> 142 AP UniProt: In Ref. 1; CAA23565..
186 -> 189 PLVQ UniProt: In Ref. 1; CAA23565..

 
Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.1 - amino acid -activation
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
GO:0016020 - membrane
GO:0009328 - phenylalanine-tRNA ligase complex
molecular_function GO:0005515 - protein binding
GO:0046872 - metal ion binding
GO:0016874 - ligase activity
GO:0004812 - aminoacyl-tRNA ligase activity
GO:0004826 - phenylalanine-tRNA ligase activity
GO:0003723 - RNA binding
GO:0000049 - tRNA binding
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0000287 - magnesium ion binding
GO:0042802 - identical protein binding
biological_process GO:0006412 - translation
GO:0006432 - phenylalanyl-tRNA aminoacylation
Note(s): Note(s): ...[more].
Reference(s): [1] Comer MM., et al., 1976
[2] Russell RR., et al., 1971
External database links:  
ALPHAFOLD:
 P07395
DIP:
 DIP-6879N
ECOCYC:
 PHET-MONOMER
ECOLIWIKI:
 b1713
INTERPRO:
 IPR020825
INTERPRO:
 IPR012340
INTERPRO:
 IPR009061
INTERPRO:
 IPR002547
INTERPRO:
 IPR005147
INTERPRO:
 IPR033714
INTERPRO:
 IPR005121
INTERPRO:
 IPR036690
INTERPRO:
 IPR004532
INTERPRO:
 IPR005146
INTERPRO:
 IPR041616
MODBASE:
 P07395
PDB:
 3PCO
PDB:
 6P24
PFAM:
 PF01588
PFAM:
 PF03147
PFAM:
 PF03483
PFAM:
 PF03484
PFAM:
 PF17759
PRIDE:
 P07395
PROSITE:
 PS51483
PROSITE:
 PS51447
PROSITE:
 PS50886
REFSEQ:
 NP_416228
SMART:
 SM00873
SMART:
 SM00896
SMART:
 SM00874
SMR:
 P07395
UNIPROT:
 P07395


Operon      
Name: thrS-infC-rpmI-rplT-pheMST-ihfA         
Operon arrangement:
Transcription unit        Promoter
ihfA
pheM
pheMST-ihfA
rplT
rplT-pheM
rpmI-rplT
infC-rpmI-rplT
infC
thrS-infC
thrS-infC-rpmI-rplT-pheMST-ihfA


Transcriptional Regulation      
Display Regulation             
Repressed by: NsrR


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_2003 1795497 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2004 1795523 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2005 1795580 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2006 1795720 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2007 1795767 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2008 1795965 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2009 1797601 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2010 1798580 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_2011 1798597 reverse nd [RS-EPT-CBR] [3]


Evidence    

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


Reference(s)    

 [1] Comer MM., Bock A., 1976, Genes for the alpha and beta subunits of the phenylalanyl-transfer ribonucleic acid synthetase of Escherichia coli., J Bacteriol 127(2):923-33

 [2] Russell RR., Pittard AJ., 1971, Mutants of Escherichia coli unable to make protein at 42 C., J Bacteriol 108(2):790-8

 [3] 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.

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