ID   SYE1_RICBR              Reviewed;         445 AA.
AC   Q1RIM2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Glutamyl-tRNA synthetase 1;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamate--tRNA ligase 1;
DE            Short=GluRS 1;
GN   Name=gltX1; OrderedLocusNames=RBE_0711;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a
CC       two-step reaction: glutamate is first activated by ATP to form
CC       Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000087; ABE04792.1; -; Genomic_DNA.
DR   RefSeq; YP_537881.1; -.
DR   GeneID; 3995311; -.
DR   GenomeReviews; CP000087_GR; RBE_0711.
DR   KEGG; rbe:RBE_0711; -.
DR   HOGENOM; Q1RIM2; -.
DR   OMA; Q1RIM2; LRLDDTD.
DR   BioCyc; RBEL336407:RBE_0711-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00022; -; 1.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-synth_Ic_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Gene3D; G3DSA:1.10.10.350; tRNA_synt_bd; 1.
DR   PANTHER; PTHR10119; Glu_tRNA-synt_1c; 1.
DR   TIGRFAMs; TIGR00464; gltX_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    445       Glutamyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000277971.
FT   MOTIF        10     20       "HIGH" region.
FT   MOTIF       240    244       "KMSKS" region.
FT   BINDING     243    243       ATP (By similarity).
SQ   SEQUENCE   445 AA;  51851 MW;  30EBB08D2FBF8905 CRC64;
     MTKVITRFAP SPTGMLHVGN IRAALLNWLY AKKHDGQFIL RFDDTDLERS KQEYKDAIRA
     DLKFLNLNWD QTFNQLSRLS RYDEIKKLLL DKKRLYACYE TPEELELKRK FQLSKGLPPI
     YDRAALNLTE DQIQKYIEQG RKPHYRFLVN HEPITWHDMI KGEVKYEGKA LSDPIVIRAD
     GSMTYMLCSV IDDVDYEITH IIRGEDHVSN TAIQIQMFEA LDKYPPTFGH LSLIINKDEK
     ISKRVGGFEI ATLREEVGLE AMAIASFFSL LGSSAQIIPH KKMDELVKHF EISSFSKSPT
     IYQPEDLERL NHKLLISLEF NEVKDRLKEI DAEYIDENFW LSVRPNLKKL FDAKDWWEIC
     HKTPNIQDLN LDKEYLKQAA ELLPEEEITT ETWGIWTKKL AAITNRKGKE LFLPLRLALT
     GKESGPEISK VLPLIKREEI VKRLT
//