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). ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu) Binds 1 zinc ion per subunit. Inhibited by 1,10-phenanthroline (PubMed:8218204). Phosphorylation of Ser-239 by HipA inhibits aminoacylation of tRNA(Glu) (PubMed:24095282, PubMed:24343429). Monomer. Phosphorylated by HipA on Ser-239 in the presence but not absence of tRNA(Glu). Phosphorylated protein cannot aminoacylate tRNA(Glu). Phosphorylated. 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. Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.