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P99170

- SYE_STAAN

UniProt

P99170 - SYE_STAAN

Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei255 – 2551ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
    3. 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, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSAUR158879:GJCB-520-MONOMER.

    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:SA0486
    OrganismiStaphylococcus aureus (strain N315)
    Taxonomic identifieri158879 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000751: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 484484Glutamate--tRNA ligasePRO_0000119653Add
    BLAST

    Proteomic databases

    PRIDEiP99170.

    2D gel databases

    SWISS-2DPAGEP99170.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi158879.SA0486.

    Structurei

    3D structure databases

    ProteinModelPortaliP99170.
    SMRiP99170. 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.
    OMAiKHYDGDF.
    OrthoDBiEOG6DRPF7.

    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.

    P99170-1 [UniParc]FASTAAdd to Basket

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    MSDRIRVRYA PSPTGYLHIG NARTALFNYL YAKHYNGDFV IRIEDTDKKR    50
    NLEDGETSQF DNLKWLGLDW DESVDKDNGY GPYRQSERQH IYQPLIDQLL 100
    AEDKAYKCYM TEEELEAERE AQIARGEMPR YGGQHAHLTE EQRQQFEAEG 150
    RQPSIRFRVP QNQTYSFDDM VKGNISFDSN GIGDWVIVKK DGIPTYNFAV 200
    AIDDHYMQIS DVIRGDDHIS NTPKQIMIYE AFGWEPPRFG HMSLIVNEER 250
    KKLSKRDGQI LQFIEQYRDL GYLPEALFNF IALLGWSPEG EEEIFSKEEF 300
    IKIFDEKRLS KSPAFFDKQK LAWVNNQYMK QKDTETVFQL ALPHLIKANL 350
    IPEVPSEEDL SWGRKLIALY QKEMSYAGEI VPLSEMFFKE MPALGEEEQQ 400
    VINGEQVPEL MTHLFSKLEA LEPFEAAEIK KTIKEVQKET GIKGKQLFMP 450
    IRVAVTGQMH GPELPNTIEV LGKEKVLNRL KQYK 484
    Length:484
    Mass (Da):56,289
    Last modified:October 11, 2004 - v1
    Checksum:i4CBA5FF08DA23EFA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB41716.1.
    PIRiA89820.
    RefSeqiNP_373738.1. NC_002745.2.

    Genome annotation databases

    EnsemblBacteriaiBAB41716; BAB41716; BAB41716.
    GeneIDi1123290.
    KEGGisau:SA0486.
    PATRICi19573082. VBIStaAur116463_0511.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000018 Genomic DNA. Translation: BAB41716.1 .
    PIRi A89820.
    RefSeqi NP_373738.1. NC_002745.2.

    3D structure databases

    ProteinModelPortali P99170.
    SMRi P99170. Positions 5-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158879.SA0486.

    2D gel databases

    SWISS-2DPAGE P99170.

    Proteomic databases

    PRIDEi P99170.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB41716 ; BAB41716 ; BAB41716 .
    GeneIDi 1123290.
    KEGGi sau:SA0486.
    PATRICi 19573082. VBIStaAur116463_0511.

    Phylogenomic databases

    eggNOGi COG0008.
    HOGENOMi HOG000252720.
    KOi K09698.
    OMAi KHYDGDF.
    OrthoDBi EOG6DRPF7.

    Enzyme and pathway databases

    BioCyci SAUR158879:GJCB-520-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: N315.
    2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: N315.
    3. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
      Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
      Submitted (OCT-2007) to UniProtKB
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: N315.

    Entry informationi

    Entry nameiSYE_STAAN
    AccessioniPrimary (citable) accession number: P99170
    Secondary accession number(s): Q99W75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 69 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

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3