ID   SYE2_RICBR              Reviewed;         464 AA.
AC   Q1RJC6;
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 2;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamate--tRNA ligase 2;
DE            Short=GluRS 2;
GN   Name=gltX2; OrderedLocusNames=RBE_0457;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000087; ABE04538.1; -; Genomic_DNA.
DR   RefSeq; YP_537627.1; -.
DR   GeneID; 3996031; -.
DR   GenomeReviews; CP000087_GR; RBE_0457.
DR   KEGG; rbe:RBE_0457; -.
DR   HOGENOM; Q1RJC6; -.
DR   OMA; Q1RJC6; IEWFNLD.
DR   BioCyc; RBEL336407:RBE_0457-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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    464       Glutamyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000277972.
FT   MOTIF        11     21       "HIGH" region.
FT   MOTIF       240    244       "KMSKS" region.
FT   BINDING     243    243       ATP (By similarity).
SQ   SEQUENCE   464 AA;  52642 MW;  3287F4E1269D22A0 CRC64;
     MTNNVITRFA PSPTGFLHIG SARTALFNYL FAKHNNGKFL LRIEDTDKER STEAAVEAIF
     SGLKWLGLNW DDEVVFQSKR NDLYKEAALK LLAEGKAYYC FTPQEEIEKQ RQEALENKQH
     FIFNSKWRDK TSDTYPKDIK PVIRLKTPSS GSITIHDTLQ GDVVIENCHI DDMVLLRSDG
     TATYMLAVVV DDHDMGITHI IRGDDHLTNA ARQIAIYNAF GYHVPIMTHI PLIHGADGAK
     LSKRHGALGV EAYKDMGYLP ESLCNYLLRL GWSHGDDEII QMDQAIEWFN LDSLGKSPAR
     LDFTKMNSLN SHYLRMLDED SLITKILEIL NRNYKVSEQE VNYIRRGLQG LLVRSETLLD
     LAKLAKIYLV NIPVAYESEA KEIIANCDKN LINNVVQGLE KLERFDKESV QDEFKKIAAA
     NSLKLNEVMK PVRALITGMV GSPSVFEIAE ILGKENILKR LEIK
//