ID   SYE1_CAMJJ              Reviewed;         431 AA.
AC   A1VZI8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Glutamate--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            Short=GluRS 1 {ECO:0000255|HAMAP-Rule:MF_00022};
GN   Name=gltX1 {ECO:0000255|HAMAP-Rule:MF_00022};
GN   OrderedLocusNames=CJJ81176_0861;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000538; EAQ72283.1; -; Genomic_DNA.
DR   RefSeq; WP_002856800.1; NC_008787.1.
DR   AlphaFoldDB; A1VZI8; -.
DR   SMR; A1VZI8; -.
DR   STRING; 354242.CJJ81176_0861; -.
DR   EnsemblBacteria; EAQ72283; EAQ72283; CJJ81176_0861.
DR   KEGG; cjj:CJJ81176_0861; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_0_7; -.
DR   OMA; NFACACD; -.
DR   Proteomes; UP000000646; 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..431
FT                   /note="Glutamate--tRNA ligase 1"
FT                   /id="PRO_0000367640"
FT   MOTIF           6..16
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           235..239
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   431 AA;  50103 MW;  E5FDDDDE8FC24A2E CRC64;
     MYRFAPSPTG DMHIGNLRAA IFNYICARQK NMDFILRIED TDKARNIAGK EEEIKEILNL
     FGISWQHYYI QSENLKFHRQ MALKLVSEKK AFACFCTEEE LEAKKELAKK QGKAYRYDGT
     CEKLADIDVL ECEKPFVIRL KKPTHTMKFT DFIKGELSFE PENIDSFVIM RTDKTPTYNF
     ACAVDDMLEN VTCIIRGEDH VSNTPKQEHI RASLGYNKAM TYAHLPIILN EEGVKMSKRE
     AHSSVKWLLE SGILPSAIAN YLIMLGNKTP CEIFTLEEAI KWFDISKVSK APARFDLKKL
     LQINREHIKM IKDDELNKIL DLNKDLAQLA KFYTQEASTI KELKEKMRAI FNTKDFGEFE
     TECKILKELL KDIELFENYE DFKNELLSKS DLKGKKFFMP LRIILTGNIH GPELSDLYPY
     IKNFIHELAR I