P04805 · SYE_ECOLI
- ProteinGlutamate--tRNA ligase
- GenegltX
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids471 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Cofactor
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).
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 μM | tRNA(Glu) | |||||
0.105 mM | Glu |
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | glutamate-tRNA ligase activity | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | glutamyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamate--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP04805
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 98 | 10-fold decrease in activity. Strong decrease in zinc content. | ||||
Sequence: C → S | ||||||
Mutagenesis | 100 | Loss of activity. Strong decrease in zinc content. | ||||
Sequence: C → S | ||||||
Mutagenesis | 100 | Does 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). | ||||
Sequence: C → Y | ||||||
Mutagenesis | 125 | Loss of activity. Strong decrease in zinc content. | ||||
Sequence: C → S | ||||||
Mutagenesis | 127 | 10-fold decrease in activity. Strong decrease in zinc content. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 129 | No change in activity or in zinc content. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 131 | No change in activity or in zinc content. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 132 | No change in activity or in zinc content. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 138 | No change in activity or in zinc content. | ||||
Sequence: C → S | ||||||
Mutagenesis | 239 | Does not aminoacylate tRNA(Glu), not phosphorylated by HipA. | ||||
Sequence: S → D |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000119555 | 1-471 | Glutamate--tRNA ligase | |||
Sequence: MKIKTRFAPSPTGYLHVGGARTALYSWLFARNHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLSLEWDEGPYYQTKRFDRYNAVIDQMLEEGTAYKCYCSKERLEALREEQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQEGSVVFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALKAPVPVYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSHGDQEIFTREEMIKYFTLNAVSKSASAFNTDKLLWLNHHYINALPPEYVATHLQWHIEQENIDTRNGPQLADLVKLLGERCKTLKEMAQSCRYFYEDFAEFDADAAKKHLRPVARQPLEVVRDKLAAITDWTAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALDFIAERENQQ | ||||||
Modified residue | 239 | Phosphoserine | ||||
Sequence: S |
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
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Monomer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P04805 | ydfR P76160 | 2 | EBI-549949, EBI-544071 |
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 9-19 | 'HIGH' region | ||||
Sequence: PSPTGYLHVGG | ||||||
Motif | 237-241 | 'KMSKS' region | ||||
Sequence: KLSKR |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length471
- Mass (Da)53,816
- Last updated1987-08-13 v1
- Checksum8264A799E5383398
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |