ID   SYE1_RICFE              Reviewed;         447 AA.
AC   Q4UM43;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=RF_0529;
OS   Rickettsia felis (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=42862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61380.1; -; Genomic_DNA.
DR   RefSeq; YP_246545.1; -.
DR   GeneID; 3401191; -.
DR   GenomeReviews; CP000053_GR; RF_0529.
DR   KEGG; rfe:RF_0529; -.
DR   NMPDR; fig|315456.3.peg.363; -.
DR   HOGENOM; Q4UM43; -.
DR   OMA; Q4UM43; LRLDDTD.
DR   BioCyc; RFEL315456:RF_0529-MON; -.
DR   BRENDA; 6.1.1.17; 297363.
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    447       Glutamyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000237396.
FT   MOTIF        10     20       "HIGH" region.
FT   MOTIF       240    244       "KMSKS" region.
FT   BINDING     243    243       ATP (By similarity).
SQ   SEQUENCE   447 AA;  51807 MW;  55F40BD252E83667 CRC64;
     MTKIITRFAP SPTGMLHVGN IRAALLNWLY AKKHNGQFIL RFDDTDLERS KQEYKDAIEE
     DLKFLNLNWD QTFNQLSRLS RYDEIKNLLL DKKRLYACYE TPEELELKRK FQLSKGLPPI
     YDRASLNLTE EQTQKYIEQG RKPHYRFLVN HEPISWHDMI KGEVKYDGKA LSEPIVIRAD
     GSMTYMLCSV IDDIDYDITH IIRGEDHVSN TAIQIQMFEA LNTTPPTFGH LSLIINKDEK
     ISKRVGGFEI TTLRKEIGLE AMAIASFFSL LGSSAQILPY KSMEKLANQF EISSFSKSPT
     IYQPEDLERL NHKLLISLDF DEVKNHLKEI DAEYIDENFW LSVRPNLQKL RDVKDWWEIC
     HKTPNVKSLN LDKEYLKQAA EVLPQGKITK DSWSIWTKEI TNITGKKGKE LFLPLRLALT
     GRESGPEIAS VLPLIDREEI IKRLTSA
//