RegulonDB RegulonDB 10.9: Gene Form
   

tyrS gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

tyrS pdxY pdxH anti-anti-terminator anti-terminator terminator terminator TSS_1915 TSS_1915 TSS_1914 TSS_1914 tyrSp2 tyrSp2 tyrSp1 tyrSp1 TSS_1913 TSS_1913

Gene      
Name: tyrS    Texpresso search in the literature
Synonym(s): ECK1633, EG11043, b1637
Genome position(nucleotides): 1715948 <-- 1717222 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 51.53
External database links:  
ASAP:
 ABE-0005477
CGSC:
 54
ECHOBASE:
 EB1036
ECOLIHUB:
 tyrS
MIM:
 613561
OU-MICROARRAY:
 b1637
STRING:
 511145.b1637
COLOMBOS: tyrS


Product      
Name: tyrosine—tRNA ligase
Synonym(s): TyrS
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 47.527
Isoelectric point: 5.55
Motif(s):
 
Type Positions Sequence
235 -> 239 KFGKT
42 -> 51 PTADSLHLGH
37 -> 37 Y
130 -> 130 F
31 -> 328 QGPIALYCGFDPTADSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNREDQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLQAAKRITECLF

 
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
molecular_function GO:0016874 - ligase activity
GO:0004812 - aminoacyl-tRNA ligase activity
GO:0003723 - RNA binding
GO:0004831 - tyrosine-tRNA ligase activity
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0042803 - protein homodimerization activity
biological_process GO:0006412 - translation
GO:0006418 - tRNA aminoacylation for protein translation
GO:0043039 - tRNA aminoacylation
GO:0006437 - tyrosyl-tRNA aminoacylation
Note(s): Note(s): ...[more].
Reference(s): [1] Abelson J., et al., 1969
[2] Airas RK. 2007
[3] Druart K., et al., 2017
[4] Mohler K., et al., 2017
[5] Simonson T., et al., 2016
[6] Skupinska M., et al., 2017
[7] Wang XD., et al., 2013
[8] Wang XD., et al., 2014
External database links:  
DIP:
 DIP-36227N
ECOCYC:
 TYRS-MONOMER
ECOLIWIKI:
 b1637
INTERPRO:
 IPR002307
INTERPRO:
 IPR002942
INTERPRO:
 IPR001412
INTERPRO:
 IPR002305
INTERPRO:
 IPR024088
INTERPRO:
 IPR024107
INTERPRO:
 IPR036986
INTERPRO:
 IPR014729
PANTHER:
 PTHR11766
PDB:
 6I5Y
PDB:
 1VBN
PDB:
 6HB6
PDB:
 6HB5
PDB:
 2YXN
PDB:
 1X8X
PDB:
 1VBM
PDB:
 6HB7
PDB:
 1WQ3
PDB:
 1WQ4
PFAM:
 PF00579
PFAM:
 PF01479
PRIDE:
 P0AGJ9
PRINTS:
 PR01040
PRODB:
 PRO_000024154
PROSITE:
 PS50889
PROSITE:
 PS00178
REFSEQ:
 NP_416154
SMART:
 SM00363
SMR:
 P0AGJ9
SWISSMODEL:
 P0AGJ9
UNIPROT:
 P0AGJ9


Operon      
Name: pdxH-tyrS-pdxY         
Operon arrangement:
Transcription unit        Promoter
tyrS-pdxY
tyrS-pdxY
pdxH-tyrS-pdxY
pdxY


RNA cis-regulatory element    
Attenuation: Translational


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_1913 1716884 reverse nd [RS-EPT-CBR] [9]
  promoter TSS_1914 1717287 reverse nd [RS-EPT-CBR] [9]
  promoter TSS_1915 1717731 reverse nd [RS-EPT-CBR] [9]


Evidence    

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


Reference(s)    

 [1] Abelson J., Barnett L., Brenner S., Gefter M., Landy A., Russell R., Smith JD., 1969, Mutant tyrosine transfer ribonucleic acids., FEBS Lett 3(1):1-4

 [2] Airas RK., 2007, Magnesium dependence of the measured equilibrium constants of aminoacyl-tRNA synthetases., Biophys Chem 131(1-3):29-35

 [3] Druart K., Guennec ML., Palmai Z., Simonson T., 2017, Probing the stereospecificity of tyrosyl- and glutaminyl-tRNA synthetase with molecular dynamics., J Mol Graph Model 71:192-199

 [4] Mohler K., Mann R., Ibba M., 2017, Isoacceptor specific characterization of tRNA aminoacylation and misacylation in vivo., Methods 113:127-131

 [5] Simonson T., Ye-Lehmann S., Palmai Z., Amara N., Wydau-Dematteis S., Bigan E., Druart K., Moch C., Plateau P., 2016, Redesigning the stereospecificity of tyrosyl-tRNA synthetase., Proteins 84(2):240-53

 [6] Skupinska M., Stepniak P., Letowska I., Rychlewski L., Barciszewska M., Barciszewski J., Giel-Pietraszuk M., 2017, Natural Compounds as Inhibitors of Tyrosyl-tRNA Synthetase., Microb Drug Resist 23(3):308-320

 [7] Wang XD., Deng RC., Dong JJ., Peng ZY., Gao XM., Li ST., Lin WQ., Lu CL., Xiao ZP., Zhu HL., 2013, 3-Aryl-4-acyloxyethoxyfuran-2(5H)-ones as inhibitors of tyrosyl-tRNA synthetase: synthesis, molecular docking and antibacterial evaluation., Bioorg Med Chem 21(17):4914-22

 [8] Wang XD., Wei W., Wang PF., Tang YT., Deng RC., Li B., Zhou SS., Zhang JW., Zhang L., Xiao ZP., Ouyang H., Zhu HL., 2014, Novel 3-arylfuran-2(5H)-one-fluoroquinolone hybrid: design, synthesis and evaluation as antibacterial agent., Bioorg Med Chem 22(14):3620-8

 [9] 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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