ID   SYE2_HELPY              Reviewed;         439 AA.
AC   O25360;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=HP_0643;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=13679580; DOI=10.1073/pnas.1932482100;
RA   Skouloubris S., Ribas de Pouplana L., de Reuse H., Hendrickson T.L.;
RT   "A noncognate aminoacyl-tRNA synthetase that may resolve a missing link in
RT   protein evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11297-11302(2003).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=14615592; DOI=10.1073/pnas.1936123100;
RA   Salazar J.C., Ahel I., Orellana O., Tumbula-Hansen D., Krieger R.,
RA   Daniels L., Soell D.;
RT   "Coevolution of an aminoacyl-tRNA synthetase with its tRNA substrates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13863-13868(2003).
CC   -!- FUNCTION: Aminoacylates tRNA(Gln) with glutamate. Does not aminoacylate
CC       tRNA(Glu). {ECO:0000269|PubMed:13679580, ECO:0000269|PubMed:14615592}.
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; AE000511; AAD07704.1; -; Genomic_DNA.
DR   PIR; C64600; C64600.
DR   RefSeq; NP_207437.1; NC_000915.1.
DR   RefSeq; WP_000943321.1; NC_000915.1.
DR   AlphaFoldDB; O25360; -.
DR   SMR; O25360; -.
DR   DIP; DIP-3622N; -.
DR   IntAct; O25360; 2.
DR   MINT; O25360; -.
DR   STRING; 85962.C694_03325; -.
DR   PaxDb; O25360; -.
DR   EnsemblBacteria; AAD07704; AAD07704; HP_0643.
DR   KEGG; hpy:HP_0643; -.
DR   PATRIC; fig|85962.8.peg.674; -.
DR   eggNOG; COG0008; Bacteria.
DR   OMA; NFACACD; -.
DR   PhylomeDB; O25360; -.
DR   BRENDA; 6.1.1.24; 2604.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..439
FT                   /note="GlutamylGlutaminyl-tRNA synthetase"
FT                   /id="PRO_0000119577"
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;  51003 MW;  9819BA3C49F60C9A CRC64;
     MLRFAPSPTG DMHIGNLRAA IFNYIVAKQQ YKPFLIRIED TDKERNIEGK DQEILEILKL
     MGISWDKLVY QSHNIDYHRE MAEKLLKENK AFYCYASAEF LEREKEKAKN EKRPFRYSDE
     WATLEKDKHH APVVRLKAPN HAVSFNDAIK KEVKFEPDEL DSFVLLRQDK SPTYNFACAC
     DDLLYKISLI IRGEDHVSNT PKQILIQQAL GSNDPIVYAH LPIILDEVSG KKMSKRDEAS
     SVKWLLNQGF LPVAIANYLI TIGNKVPKEV FSLDEAIEWF SLENLSSSPA HFNLKYLKHL
     NHEHLKLLDD DKLLELTSIK DKNLLGLLRL FIEECGTLLE LREKISLFLE PKDIVKTYEN
     EDFKERCLAL FNALTSMDFQ AYKDFESFKK EAMRLSQLKG KDFFKPLRIL LTGNSHGVEL
     PLIFPYIQSH HQEVLRLKA