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P04805

- SYE_ECOLI

UniProt

P04805 - SYE_ECOLI

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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).1 Publication

Cofactori

Binds 1 zinc ion per subunit.2 Publications

Enzyme regulationi

Inhibited by 1,10-phenanthroline. Phosphorylation of Ser-239 by HipA inhibits aminoacylation of tRNA(Glu).2 Publications

Kineticsi

  1. KM=0.32 µM for tRNA(Glu)1 Publication
  2. KM=0.105 mM for Glu1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi98 – 981Zinc
Metal bindingi100 – 1001Zinc
Metal bindingi125 – 1251Zinc
Metal bindingi127 – 1271Zinc
Binding sitei240 – 2401ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: EcoCyc
  3. tRNA binding Source: InterPro
  4. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Gene namesi
Name:gltX
Ordered Locus Names:b2400, JW2395
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10407. gltX.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi98 – 981C → S: 10-fold decrease in activity. Strong decrease in zinc content. 1 Publication
Mutagenesisi100 – 1001C → S: Loss of activity. Strong decrease in zinc content. 2 Publications
Mutagenesisi100 – 1001C → 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). 2 Publications
Mutagenesisi125 – 1251C → S: Loss of activity. Strong decrease in zinc content. 1 Publication
Mutagenesisi127 – 1271H → Q: 10-fold decrease in activity. Strong decrease in zinc content. 1 Publication
Mutagenesisi129 – 1291H → Q: No change in activity or in zinc content. 1 Publication
Mutagenesisi131 – 1311H → Q: No change in activity or in zinc content. 1 Publication
Mutagenesisi132 – 1321H → Q: No change in activity or in zinc content. 1 Publication
Mutagenesisi138 – 1381C → S: No change in activity or in zinc content. 1 Publication
Mutagenesisi239 – 2391S → D: Does not aminoacylate tRNA(Glu), not phosphorylated by HipA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Glutamate--tRNA ligasePRO_0000119555Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by HipA on Ser-239 in the presence but not absence of tRNA(Glu). Phosphorylated protein cannot aminoacylate tRNA(Glu).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP04805.
PRIDEiP04805.

Expressioni

Gene expression databases

GenevestigatoriP04805.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

DIPiDIP-9810N.
IntActiP04805. 16 interactions.
MINTiMINT-1296746.
STRINGi511145.b2400.

Structurei

3D structure databases

ProteinModelPortaliP04805.
SMRiP04805. Positions 3-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionAdd
BLAST
Motifi237 – 2415"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
InParanoidiP04805.
KOiK01885.
OMAiDSHEHHA.
OrthoDBiEOG6DRPF7.
PhylomeDBiP04805.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04805-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RNHGGEFVLR IEDTDLERST
60 70 80 90 100
PEAIEAIMDG MNWLSLEWDE GPYYQTKRFD RYNAVIDQML EEGTAYKCYC
110 120 130 140 150
SKERLEALRE EQMAKGEKPR YDGRCRHSHE HHADDEPCVV RFANPQEGSV
160 170 180 190 200
VFDDQIRGPI EFSNQELDDL IIRRTDGSPT YNFCVVVDDW DMEITHVIRG
210 220 230 240 250
EDHINNTPRQ INILKALKAP VPVYAHVSMI NGDDGKKLSK RHGAVSVMQY
260 270 280 290 300
RDDGYLPEAL LNYLVRLGWS HGDQEIFTRE EMIKYFTLNA VSKSASAFNT
310 320 330 340 350
DKLLWLNHHY INALPPEYVA THLQWHIEQE NIDTRNGPQL ADLVKLLGER
360 370 380 390 400
CKTLKEMAQS CRYFYEDFAE FDADAAKKHL RPVARQPLEV VRDKLAAITD
410 420 430 440 450
WTAENVHHAI QATADELEVG MGKVGMPLRV AVTGAGQSPA LDVTVHAIGK
460 470
TRSIERINKA LDFIAERENQ Q
Length:471
Mass (Da):53,816
Last modified:August 13, 1987 - v1
Checksum:i8264A799E5383398
GO

Mass spectrometryi

Molecular mass is 56224.09 Da from positions 1 - 471. Determined by MALDI. 1 Publication
Molecular mass is 56304.11 Da from positions 1 - 471. Determined by MALDI. Phosphorylated.1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA25956. SYECET.
RefSeqiNP_416899.1. NC_000913.3.
YP_490639.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75457; AAC75457; b2400.
BAA16272; BAA16272; BAA16272.
GeneIDi12930199.
946906.
KEGGiecj:Y75_p2364.
eco:b2400.
PATRICi32120177. VBIEscCol129921_2495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A25956. SYECET.
RefSeqi NP_416899.1. NC_000913.3.
YP_490639.1. NC_007779.1.

3D structure databases

ProteinModelPortali P04805.
SMRi P04805. Positions 3-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9810N.
IntActi P04805. 16 interactions.
MINTi MINT-1296746.
STRINGi 511145.b2400.

Chemistry

BindingDBi P04805.

Proteomic databases

PaxDbi P04805.
PRIDEi P04805.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75457 ; AAC75457 ; b2400 .
BAA16272 ; BAA16272 ; BAA16272 .
GeneIDi 12930199.
946906.
KEGGi ecj:Y75_p2364.
eco:b2400.
PATRICi 32120177. VBIEscCol129921_2495.

Organism-specific databases

EchoBASEi EB0402.
EcoGenei EG10407. gltX.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252722.
InParanoidi P04805.
KOi K01885.
OMAi DSHEHHA.
OrthoDBi EOG6DRPF7.
PhylomeDBi P04805.

Enzyme and pathway databases

BioCyci EcoCyc:GLURS-MONOMER.
ECOL316407:JW2395-MONOMER.
MetaCyc:GLURS-MONOMER.
SABIO-RK P04805.

Miscellaneous databases

PROi P04805.

Gene expression databases

Genevestigatori P04805.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi IPR008925. 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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF00749. tRNA-synt_1c. 1 hit.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF48163. SSF48163. 1 hit.
TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSYE_ECOLI
AccessioniPrimary (citable) accession number: P04805
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3