RegulonDB RegulonDB 11.1: Gene Form
   

gltX gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

gltX yfeD valU Fis Fis Fis terminator valUp valUp TSS_2687 TSS_2687 gltXp1 gltXp1 gltXp2 gltXp2 TSS_2685 (cluster) TSS_2685 (cluster) gltXp3 gltXp3 TSS_2683 TSS_2683 TSS_2682 TSS_2682

Gene      
Name: gltX    Texpresso search in the literature
Synonym(s): ECK2394, EG10407, b2400, gltM, gluRS
Genome position(nucleotides): 2519257 <-- 2520672
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 52.54
External database links:  
ASAP:
 ABE-0007911
CGSC:
 676
ECHOBASE:
 EB0402
ECOLIHUB:
 gltX
MIM:
 614924
OU-MICROARRAY:
 b2400
STRING:
 511145.b2400
COLOMBOS: gltX


Product      
Name: glutamate—tRNA ligase
Synonym(s): GltM, GltX, GluRS
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 53.816
Isoelectric point: 5.804
Motif(s):
 
Type Positions Sequence Comment
2 -> 305 KIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLW
9 -> 19 PSPTGYLHVGG UniProt: 'HIGH' region; Sequence Annotation Type: short sequence motif.
98 -> 98 C UniProt: 10-fold decrease in activity. Strong decrease in zinc content..
100 -> 100 C UniProt: Loss of activity. Strong decrease in zinc content..
125 -> 125 C UniProt: Loss of activity. Strong decrease in zinc content..

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.3 - cofactors, small molecule carriers --> 1.5.3.12 - heme, porphyrine
  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:0005515 - protein binding
GO:0046872 - metal ion binding
GO:0016874 - ligase activity
GO:0004812 - aminoacyl-tRNA ligase activity
GO:0000049 - tRNA binding
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0008270 - zinc ion binding
GO:0004818 - glutamate-tRNA ligase activity
biological_process GO:0006412 - translation
GO:0006418 - tRNA aminoacylation for protein translation
GO:0043039 - tRNA aminoacylation
GO:0006779 - porphyrin-containing compound biosynthetic process
GO:0006424 - glutamyl-tRNA aminoacylation
Note(s): Note(s): ...[more].
Reference(s): [1] Blais SP., et al., 2015
[2] Breton R., et al., 1986
[3] Chongdar N., et al., 2014
[4] Chongdar N., et al., 2015
[5] Van de Vijver P., et al., 2009
External database links:  
ALPHAFOLD:
 P04805
DIP:
 DIP-9810N
ECOCYC:
 GLURS-MONOMER
ECOLIWIKI:
 b2400
INTERPRO:
 IPR008925
INTERPRO:
 IPR020058
INTERPRO:
 IPR020751
INTERPRO:
 IPR033910
INTERPRO:
 IPR000924
INTERPRO:
 IPR014729
INTERPRO:
 IPR004527
INTERPRO:
 IPR001412
MODBASE:
 P04805
PFAM:
 PF00749
PFAM:
 PF19269
PRIDE:
 P04805
PRINTS:
 PR00987
PRODB:
 PRO_000022813
PROSITE:
 PS00178
REFSEQ:
 NP_416899
SMR:
 P04805
UNIPROT:
 P04805


Operon      
Name: gltX         
Operon arrangement:
Transcription unit        Promoter
gltX
gltX
gltX


Transcriptional Regulation      
Display Regulation             
Repressed by: Fis


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_2682 2519911 reverse nd [RS-EPT-CBR] [6]
  promoter TSS_2683 2520714 reverse nd [RS-EPT-CBR] [6]
  promoter TSS_2685 (cluster) 2520775 reverse nd [RS-EPT-CBR] [6]
  promoter TSS_2687 2520922 forward nd [RS-EPT-CBR] [6]


Evidence    

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


Reference(s)    

 [1] Blais SP., Kornblatt JA., Barbeau X., Bonnaure G., Lague P., Chenevert R., Lapointe J., 2015, tRNAGlu increases the affinity of glutamyl-tRNA synthetase for its inhibitor glutamyl-sulfamoyl-adenosine, an analogue of the aminoacylation reaction intermediate glutamyl-AMP: mechanistic and evolutionary implications., PLoS One 10(4):e0121043

 [2] Breton R., Sanfacon H., Papayannopoulos I., Biemann K., Lapointe J., 1986, Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases., J Biol Chem 261(23):10610-7

 [3] Chongdar N., Dasgupta S., Datta AB., Basu G., 2014, Preliminary X-ray crystallographic analysis of an engineered glutamyl-tRNA synthetase from Escherichia coli., Acta Crystallogr F Struct Biol Commun 70(Pt 7):922-7

 [4] Chongdar N., Dasgupta S., Datta AB., Basu G., 2015, Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase., Biosci Rep 35(2)

 [5] Van de Vijver P., Vondenhoff GH., Kazakov TS., Semenova E., Kuznedelov K., Metlitskaya A., Van Aerschot A., Severinov K., 2009, Synthetic microcin C analogs targeting different aminoacyl-tRNA synthetases., J Bacteriol 191(20):6273-80

 [6] 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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