ID   SYE2_RICFE              Reviewed;         463 AA.
AC   Q4UME8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, 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=RF_0413;
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; AAY61264.1; -; Genomic_DNA.
DR   RefSeq; YP_246429.1; -.
DR   GeneID; 3400710; -.
DR   GenomeReviews; CP000053_GR; RF_0413.
DR   KEGG; rfe:RF_0413; -.
DR   NMPDR; fig|315456.3.peg.247; -.
DR   HOGENOM; Q4UME8; -.
DR   OMA; Q4UME8; IEWFNLD.
DR   BioCyc; RFEL315456:RF_0413-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; 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    463       Glutamyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000237397.
FT   MOTIF        10     20       "HIGH" region.
FT   MOTIF       239    243       "KMSKS" region.
FT   BINDING     242    242       ATP (By similarity).
SQ   SEQUENCE   463 AA;  52726 MW;  869DFB94C9DC3201 CRC64;
     MTNVITRFAP SPTGFLHIGS ARTALFNYLF ARHHNGKFLL RIEDTDKERS TKEAVEAIFS
     GLKWLGLDWD GEVIFQSKRN NLYKEAALRL LQEGKAYYCF TSQEEIERQR QKALENKQHF
     IFNSEWRDKD SSTYPTDIKP VIRLKVPREG SITIHDTLQG DVVIENSHID DMVLLRADGT
     ATYMLAVVVD DHDMGITHII RGDDHLTNAA RQIAIYHAFG YEVPSMTHIP LIHGADGAKL
     SKRHGALGVE AYKDMGYLPE SLCNYLLRLG WSHGDDEIIS MTQAIEWFNL DSLGKSPSKL
     DFAKMNSLNA HYLRMLDNDS LTSKTVEILK QNYKISEKEV SYIKQAMPSL LVRSETLLDL
     AKLARIYLIN SPIIYEQEAK EIIENCDKDL IKQVIEGLNK IEQFDKESVQ NKFKEIATHN
     GLKLNDIMKP VRALITGMTA SPSVFEIAEI LGKENILKRL KII
//