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P22250

- SYE_BACSU

UniProt

P22250 - SYE_BACSU

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      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).UniRule annotation

    Catalytic activityi

    ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi108 – 1081ZincUniRule annotation
    Metal bindingi110 – 1101ZincUniRule annotation
    Metal bindingi135 – 1351ZincUniRule annotation
    Metal bindingi137 – 1371ZincUniRule annotation
    Binding sitei255 – 2551ATPUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP

    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

    BioCyciBSUB:BSU00920-MONOMER.
    MetaCyc:MONOMER-13959.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
    Alternative name(s):
    Glutamyl-tRNA synthetaseUniRule annotation
    Short name:
    GluRSUniRule annotation
    Gene namesi
    Name:gltXUniRule annotation
    Ordered Locus Names:BSU00920
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU00920. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 483483Glutamate--tRNA ligasePRO_0000119508Add
    BLAST

    Proteomic databases

    PaxDbiP22250.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    IntActiP22250. 1 interaction.
    MINTiMINT-8366956.
    STRINGi224308.BSU00920.

    Structurei

    3D structure databases

    ProteinModelPortaliP22250.
    SMRiP22250. Positions 5-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi11 – 2111"HIGH" regionAdd
    BLAST
    Motifi252 – 2565"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0008.
    HOGENOMiHOG000252720.
    KOiK09698.
    OMAiVTGQTHG.
    OrthoDBiEOG6DRPF7.
    PhylomeDBiP22250.

    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.

    P22250-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNEVRVRYA PSPTGHLHIG NARTALFNYL FARNQGGKFI IRVEDTDKKR    50
    NIEGGEQSQL NYLKWLGIDW DESVDVGGEY GPYRQSERND IYKVYYEELL 100
    EKGLAYKCYC TEEELEKERE EQIARGEMPR YSGKHRDLTQ EEQEKFIAEG 150
    RKPSIRFRVP EGKVIAFNDI VKGEISFESD GIGDFVIVKK DGTPTYNFAV 200
    AIDDYLMKMT HVLRGEDHIS NTPKQIMIYQ AFGWDIPQFG HMTLIVNESR 250
    KKLSKRDESI IQFIEQYKEL GYLPEALFNF IGLLGWSPVG EEELFTKEQF 300
    IEIFDVNRLS KSPALFDMHK LKWVNNQYVK KLDLDQVVEL TLPHLQKAGK 350
    VGTELSAEEQ EWVRKLISLY HEQLSYGAEI VELTDLFFTD EIEYNQEAKA 400
    VLEEEQVPEV LSTFAAKLEE LEEFTPDNIK ASIKAVQKET GHKGKKLFMP 450
    IRVAVTGQTH GPELPQSIEL IGKETAIQRL KNI 483
    Length:483
    Mass (Da):55,722
    Last modified:August 1, 1991 - v1
    Checksum:iEF61671AEE465DD5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55073 Genomic DNA. Translation: AAA22495.1.
    L14580 Genomic DNA. Translation: AAA21796.1.
    D26185 Genomic DNA. Translation: BAA05326.1.
    U49789 Genomic DNA. Translation: AAC31971.1.
    AL009126 Genomic DNA. Translation: CAB11868.1.
    PIRiA36090. SYBSET.
    RefSeqiNP_387973.1. NC_000964.3.
    WP_004399675.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB11868; CAB11868; BSU00920.
    GeneIDi936862.
    KEGGibsu:BSU00920.
    PATRICi18971689. VBIBacSub10457_0093.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55073 Genomic DNA. Translation: AAA22495.1 .
    L14580 Genomic DNA. Translation: AAA21796.1 .
    D26185 Genomic DNA. Translation: BAA05326.1 .
    U49789 Genomic DNA. Translation: AAC31971.1 .
    AL009126 Genomic DNA. Translation: CAB11868.1 .
    PIRi A36090. SYBSET.
    RefSeqi NP_387973.1. NC_000964.3.
    WP_004399675.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali P22250.
    SMRi P22250. Positions 5-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P22250. 1 interaction.
    MINTi MINT-8366956.
    STRINGi 224308.BSU00920.

    Proteomic databases

    PaxDbi P22250.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB11868 ; CAB11868 ; BSU00920 .
    GeneIDi 936862.
    KEGGi bsu:BSU00920.
    PATRICi 18971689. VBIBacSub10457_0093.

    Organism-specific databases

    GenoListi BSU00920. [Micado ]

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252720.
    KOi K09698.
    OMAi VTGQTHG.
    OrthoDBi EOG6DRPF7.
    PhylomeDBi P22250.

    Enzyme and pathway databases

    BioCyci BSUB:BSU00920-MONOMER.
    MetaCyc:MONOMER-13959.

    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 synthetases of Bacillus subtilis 168T and of Bacillus stearothermophilus. Cloning and sequencing of the gltX genes and comparison with other aminoacyl-tRNA synthetases."
      Breton R., Watson D., Yaguchi M., Lapointe J.
      J. Biol. Chem. 265:18248-18255(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis."
      Gagnon Y., Breton R., Putzer H., Pelchat M., Grunberg-Manago M., Lapointe J.
      J. Biol. Chem. 269:7473-7482(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
      Ogasawara N., Nakai S., Yoshikawa H.
      DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    4. Ishino Y., Kim S.I., Soell D.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    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: COFACTOR.

    Entry informationi

    Entry nameiSYE_BACSU
    AccessioniPrimary (citable) accession number: P22250
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3