P04805 · SYE_ECOLI

Function

function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Phosphorylation of GltX by HipA prevents it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to multidrug resistance and persistence (PubMed:24095282, PubMed:24343429).
Overexpression of GltX prevents HipA-induced growth arrest, persister formation and increases in (p)ppGpp levels (PubMed:24343429, PubMed:28430938).

Miscellaneous

This is the smallest aminoacyl-tRNA synthetase of E.coli; it does not bind glutamate in the absence of cognate tRNA, which is therefore required for activation of the amino acid substrate.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Activity regulation

Inhibited by 1,10-phenanthroline (PubMed:8218204).
Phosphorylation of Ser-239 by HipA inhibits aminoacylation of tRNA(Glu) (PubMed:24095282, PubMed:24343429).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.32 μMtRNA(Glu)
0.105 mMGlu

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site98Zn2+ (UniProtKB | ChEBI)
Binding site100Zn2+ (UniProtKB | ChEBI)
Binding site125Zn2+ (UniProtKB | ChEBI)
Binding site127Zn2+ (UniProtKB | ChEBI)
Binding site240ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionglutamate-tRNA ligase activity
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processglutamyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamate--tRNA ligase
  • EC number
  • Alternative names
    • Glutamyl-tRNA synthetase
      (GluRS
      )

Gene names

    • Name
      gltX
    • Ordered locus names
      b2400, JW2395

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P04805

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis9810-fold decrease in activity. Strong decrease in zinc content.
Mutagenesis100Loss of activity. Strong decrease in zinc content.
Mutagenesis100Does not prevent zinc binding. Reduces only 2-fold the binding affinity for tRNA(Glu), but reduces more than 10-fold the affinity for glutamate in the presence of tRNA(Glu).
Mutagenesis125Loss of activity. Strong decrease in zinc content.
Mutagenesis12710-fold decrease in activity. Strong decrease in zinc content.
Mutagenesis129No change in activity or in zinc content.
Mutagenesis131No change in activity or in zinc content.
Mutagenesis132No change in activity or in zinc content.
Mutagenesis138No change in activity or in zinc content.
Mutagenesis239Does not aminoacylate tRNA(Glu), not phosphorylated by HipA.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001195551-471Glutamate--tRNA ligase
Modified residue239Phosphoserine

Post-translational modification

Phosphorylated by HipA on Ser-239 in the presence but not absence of tRNA(Glu). Phosphorylated protein cannot aminoacylate tRNA(Glu).

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Monomer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P04805ydfR P761602EBI-549949, EBI-544071

Protein-protein interaction databases

Chemistry

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif9-19'HIGH' region
Motif237-241'KMSKS' region

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    471
  • Mass (Da)
    53,816
  • Last updated
    1987-08-13 v1
  • Checksum
    8264A799E5383398
MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINALPPEYVATHLQWHIEQENIDTRNGPQLADLVKLLGERCKTLKEMAQSCRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDKLAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALDFIAERENQQ

Mass Spectrometry

Molecular mass is 56,224.09 Da. Determined by MALDI.
Molecular mass is 56,304.11 Da. Determined by MALDI. Phosphorylated.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X63976
EMBL· GenBank· DDBJ
CAA45391.1
EMBL· GenBank· DDBJ
Genomic DNA
M13687
EMBL· GenBank· DDBJ
AAA65715.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC75457.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA16272.1
EMBL· GenBank· DDBJ
Genomic DNA
X55737
EMBL· GenBank· DDBJ
CAA39269.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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