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P04805 (SYE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:b2400, JW2395
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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). Ref.7 Ref.8 Ref.12

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 ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to multidrug resistance and persistence. Ref.7 Ref.8 Ref.12

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). Ref.6

Cofactor

Binds 1 zinc ion per subunit. Ref.6 Ref.9

Enzyme regulation

Inhibited by 1,10-phenanthroline. Phosphorylation of Ser-239 by HipA inhibits aminoacylation of tRNA(Glu). Ref.6 Ref.12

Subunit structure

Monomer. Ref.1

Subcellular location

Cytoplasm HAMAP-Rule MF_00022_B.

Post-translational modification

Phosphorylated by HipA on Ser-239 in the presence but not absence of tRNA(Glu). Phosphorylated protein cannot aminoacylate tRNA(Glu). Ref.12

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.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.32 µM for tRNA(Glu) Ref.11

KM=0.105 mM for Glu

Mass spectrometry

Molecular mass is 56224.09 Da from positions 1 - 471. Determined by MALDI. Ref.12

Molecular mass is 56304.11 Da from positions 1 - 471. Determined by MALDI. Phosphorylated. Ref.12

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Glutamate--tRNA ligase HAMAP-Rule MF_00022_B
PRO_0000119555

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022_B
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Metal binding981Zinc
Metal binding1001Zinc
Metal binding1251Zinc
Metal binding1271Zinc
Binding site2401ATP By similarity

Amino acid modifications

Modified residue2391Phosphoserine HAMAP-Rule MF_00022_B

Experimental info

Mutagenesis981C → S: 10-fold decrease in activity. Strong decrease in zinc content. Ref.9
Mutagenesis1001C → S: Loss of activity. Strong decrease in zinc content. Ref.9 Ref.11
Mutagenesis1001C → Y: 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). Ref.9 Ref.11
Mutagenesis1251C → S: Loss of activity. Strong decrease in zinc content. Ref.9
Mutagenesis1271H → Q: 10-fold decrease in activity. Strong decrease in zinc content. Ref.9
Mutagenesis1291H → Q: No change in activity or in zinc content. Ref.9
Mutagenesis1311H → Q: No change in activity or in zinc content. Ref.9
Mutagenesis1321H → Q: No change in activity or in zinc content. Ref.9
Mutagenesis1381C → S: No change in activity or in zinc content. Ref.9
Mutagenesis2391S → D: Does not aminoacylate tRNA(Glu), not phosphorylated by HipA. Ref.12

Sequences

Sequence LengthMass (Da)Tools
P04805 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 8264A799E5383398

FASTA47153,816
        10         20         30         40         50         60 
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RNHGGEFVLR IEDTDLERST PEAIEAIMDG 

        70         80         90        100        110        120 
MNWLSLEWDE GPYYQTKRFD RYNAVIDQML EEGTAYKCYC SKERLEALRE EQMAKGEKPR 

       130        140        150        160        170        180 
YDGRCRHSHE HHADDEPCVV RFANPQEGSV VFDDQIRGPI EFSNQELDDL IIRRTDGSPT 

       190        200        210        220        230        240 
YNFCVVVDDW DMEITHVIRG EDHINNTPRQ INILKALKAP VPVYAHVSMI NGDDGKKLSK 

       250        260        270        280        290        300 
RHGAVSVMQY RDDGYLPEAL LNYLVRLGWS HGDQEIFTRE EMIKYFTLNA VSKSASAFNT 

       310        320        330        340        350        360 
DKLLWLNHHY INALPPEYVA THLQWHIEQE NIDTRNGPQL ADLVKLLGER CKTLKEMAQS 

       370        380        390        400        410        420 
CRYFYEDFAE FDADAAKKHL RPVARQPLEV VRDKLAAITD WTAENVHHAI QATADELEVG 

       430        440        450        460        470 
MGKVGMPLRV AVTGAGQSPA LDVTVHAIGK TRSIERINKA LDFIAERENQ Q 

« Hide

References

« Hide 'large scale' references
[1]"Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases."
Breton R., Sanfacon H., Papayannopoulos I., Biemann K., Lapointe J.
J. Biol. Chem. 261:10610-10617(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Closely spaced and divergent promoters for an aminoacyl-tRNA synthetase gene and a tRNA operon in Escherichia coli. Transcriptional and post-transcriptional regulation of gltX, valU and alaW."
Brun V., Sanfacon H., Breton R., Lapointe J.
J. Mol. Biol. 214:845-864(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
[6]"The glutamyl-tRNA synthetase of Escherichia coli contains one atom of zinc essential for its native conformation and its catalytic activity."
Liu J., Lin S.-X., Blochet J.-E., Pezolet M., Lapointe J.
Biochemistry 32:11390-11396(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 112-116, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION.
[7]"The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. Evidence for a two-step aminoacylation pathway, and study of the reactivity of the intermediate complex."
Kern D., Lapointe J.
Eur. J. Biochem. 106:137-150(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The catalytic mechanism of the glutamyl-tRNA synthetase from Escherichia coli. Detection of an intermediate complex in which glutamate is activated."
Kern D., Lapointe J.
J. Biol. Chem. 255:1956-1961(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The zinc-binding site of Escherichia coli glutamyl-tRNA synthetase is located in the acceptor-binding domain. Studies by extended x-ray absorption fine structure, molecular modeling, and site-directed mutagenesis."
Liu J., Gagnon Y., Gauthier J., Furenlid L., L'Heureux P.-J., Auger M., Nureki O., Yokoyama S., Lapointe J.
J. Biol. Chem. 270:15162-15169(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, ZINC-BINDING SITES, MUTAGENESIS OF CYS-98; CYS-100; CYS-125; HIS-127; HIS-129; HIS-131; HIS-132 AND CYS-138.
[10]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[11]"The zinc-binding site of a class I aminoacyl-tRNA synthetase is a SWIM domain that modulates amino acid binding via the tRNA acceptor arm."
Banerjee R., Dubois D.Y., Gauthier J., Lin S.-X., Roy S., Lapointe J.
Eur. J. Biochem. 271:724-733(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-100.
[12]"Molecular mechanism of bacterial persistence by HipA."
Germain E., Castro-Roa D., Zenkin N., Gerdes K.
Mol. Cell 52:248-254(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION BY HIPA, MASS SPECTROMETRY, MUTAGENESIS OF SER-239.
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63976 Genomic DNA. Translation: CAA45391.1.
M13687 Genomic DNA. Translation: AAA65715.1.
U00096 Genomic DNA. Translation: AAC75457.1.
AP009048 Genomic DNA. Translation: BAA16272.1.
X55737 Genomic DNA. Translation: CAA39269.1.
PIRSYECET. A25956.
RefSeqNP_416899.1. NC_000913.3.
YP_490639.1. NC_007779.1.

3D structure databases

ProteinModelPortalP04805.
SMRP04805. Positions 3-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9810N.
IntActP04805. 16 interactions.
MINTMINT-1296746.
STRING511145.b2400.

Chemistry

BindingDBP04805.

Proteomic databases

PaxDbP04805.
PRIDEP04805.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75457; AAC75457; b2400.
BAA16272; BAA16272; BAA16272.
GeneID12930199.
946906.
KEGGecj:Y75_p2364.
eco:b2400.
PATRIC32120177. VBIEscCol129921_2495.

Organism-specific databases

EchoBASEEB0402.
EcoGeneEG10407. gltX.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.
PhylomeDBP04805.

Enzyme and pathway databases

BioCycEcoCyc:GLURS-MONOMER.
ECOL316407:JW2395-MONOMER.
MetaCyc:GLURS-MONOMER.
SABIO-RKP04805.

Gene expression databases

GenevestigatorP04805.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP04805.

Entry information

Entry nameSYE_ECOLI
AccessionPrimary (citable) accession number: P04805
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 14, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries