ID   SYE2_RICCK              Reviewed;         445 AA.
AC   A8EZB8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Glutamate--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            Short=GluRS 2 {ECO:0000255|HAMAP-Rule:MF_00022};
GN   Name=gltX2 {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=A1E_03870;
OS   Rickettsia canadensis (strain McKiel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=293613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=McKiel;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia canadensis.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC       step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC       then transferred to the acceptor end of tRNA(Glu). {ECO:0000255|HAMAP-
CC       Rule:MF_00022}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00022};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00022}.
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DR   EMBL; CP000409; ABV73701.1; -; Genomic_DNA.
DR   RefSeq; WP_012148896.1; NC_009879.1.
DR   AlphaFoldDB; A8EZB8; -.
DR   SMR; A8EZB8; -.
DR   STRING; 293613.A1E_03870; -.
DR   EnsemblBacteria; ABV73701; ABV73701; A1E_03870.
DR   KEGG; rcm:A1E_03870; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_1_5; -.
DR   OMA; PHWRFKL; -.
DR   OrthoDB; 1409413at2; -.
DR   Proteomes; UP000007056; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR   InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; SSF48163; 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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..445
FT                   /note="Glutamate--tRNA ligase 2"
FT                   /id="PRO_0000367757"
FT   MOTIF           10..20
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           240..244
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         243
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   445 AA;  51758 MW;  FDF55EE5C69D22F0 CRC64;
     MTKVITRFAP SPTGMLHVGN IRVALLNWLY AKKHNGQFIL RFDDTDLERS KQEYKNAIEE
     DLKFLKINWD QTFNQLSRLS RYDVIKKLLL DKKRLYTCYE TPEELELKRK VQLSKGLPPI
     YDRASLNLTT EQIKKYIEQG RKPHYRFLVN HELISWHDMI KGEVKYDGKA LSDPIVIRAD
     GSMTYMLCSV IDDIDYDITH IIRGEDHVGN TAIQIQMFEA LNKIPPVFGH LSLIINKDEK
     ISKRIGGFEI ATLRKQIGLE AMAIASFFSL LGSSSQILPY KNMDELATQF EISNFSKSPT
     MYQPEDLVRL NHKLLISVDF DEVKERLKEI DATYIDENFW LSVRPNLQKL RDVKDWWDIC
     NQTPNVENLN LDKEYLKQAA ELLPQGEITK DSWRIWTKEI TNITSRKGKE LFLPLRLALT
     GRESGPEIAG ILPLIDRKEI IKRLT