ID   SYE2_HELPJ              Reviewed;         439 AA.
AC   Q9ZLJ1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=GlutamylGlutaminyl-tRNA synthetase;
DE            Short=GluGlnRS;
DE            EC=6.1.1.-;
DE   AltName: Full=Glutamate--tRNA ligase 2;
DE            Short=GluRS 2;
DE   AltName: Full=Glutamyl-tRNA synthetase 2;
GN   Name=gltX2; OrderedLocusNames=jhp_0588;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Aminoacylates tRNA(Gln) with glutamate. Does not aminoacylate
CC       tRNA(Glu) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Gln); Xref=Rhea:RHEA:51156, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9684, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily. {ECO:0000305}.
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DR   EMBL; AE001439; AAD06161.1; -; Genomic_DNA.
DR   PIR; B71913; B71913.
DR   RefSeq; WP_000943317.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZLJ1; -.
DR   SMR; Q9ZLJ1; -.
DR   STRING; 85963.jhp_0588; -.
DR   EnsemblBacteria; AAD06161; AAD06161; jhp_0588.
DR   KEGG; hpj:jhp_0588; -.
DR   PATRIC; fig|85963.30.peg.398; -.
DR   eggNOG; COG0008; Bacteria.
DR   OMA; NFACACD; -.
DR   Proteomes; UP000000804; 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..439
FT                   /note="GlutamylGlutaminyl-tRNA synthetase"
FT                   /id="PRO_0000119579"
FT   MOTIF           6..16
FT                   /note="'HIGH' region"
FT   MOTIF           232..236
FT                   /note="'KMSKS' region"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  51073 MW;  F6DA38EEDE2D6694 CRC64;
     MLRFAPSPTG DMHIGNLRAA IFNYIVAKQQ NKPFLIRIED TDKERNIEGK DREILEILKL
     MGISWDKLVY QSHNIDYHRE MAEKLLKENK AFYCYASAEF LEREKEKAKN EKRPFRYLDE
     WATLEKDKNH APVVRLKAPN HAVSFNDAIK KEVKFEPDEL DSFVLLRQDK SPTYNFACAC
     DDLLYEISLI IRGEDHVSNT PKQILIQQAL GSNDPIVYAH LPIILDETSG KKMSKRDEAS
     SVKWLLNQGF LPEAIANYLI TIGNKVPKEV FSLDEAIEWF SLENLSSSPA HFNLKYLKHL
     NHEHLKLLDD DKLLELTLIK DKNLLGLLRL FIEECGTLLE LKEKISLFLE PKDIVKTYEN
     EDFKERCLTL FNALKSMDFQ AYKDFESFKK EAMRLSQLKG KDFFKPLRIL LTGNSHGVEL
     PLIFPYIQSH HQEVLRLKA