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P04805

- SYE_ECOLI

UniProt

P04805 - SYE_ECOLI

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    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

    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-SubCell

    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.
    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

    MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RNHGGEFVLR IEDTDLERST    50
    PEAIEAIMDG MNWLSLEWDE GPYYQTKRFD RYNAVIDQML EEGTAYKCYC 100
    SKERLEALRE EQMAKGEKPR YDGRCRHSHE HHADDEPCVV RFANPQEGSV 150
    VFDDQIRGPI EFSNQELDDL IIRRTDGSPT YNFCVVVDDW DMEITHVIRG 200
    EDHINNTPRQ INILKALKAP VPVYAHVSMI NGDDGKKLSK RHGAVSVMQY 250
    RDDGYLPEAL LNYLVRLGWS HGDQEIFTRE EMIKYFTLNA VSKSASAFNT 300
    DKLLWLNHHY INALPPEYVA THLQWHIEQE NIDTRNGPQL ADLVKLLGER 350
    CKTLKEMAQS CRYFYEDFAE FDADAAKKHL RPVARQPLEV VRDKLAAITD 400
    WTAENVHHAI QATADELEVG MGKVGMPLRV AVTGAGQSPA LDVTVHAIGK 450
    TRSIERINKA LDFIAERENQ Q 471
    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.
    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

    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 1, 2014
    This is version 134 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