SYE1_RICRO
ID SYE1_RICRO Reviewed; 447 AA.
AC B0BX35;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=RrIowa_0535;
OS Rickettsia rickettsii (strain Iowa).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=452659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa;
RX PubMed=18025092; DOI=10.1128/iai.00952-07;
RA Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F.,
RA Hackstadt T.;
RT "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT avirulent Rickettsia rickettsii Iowa.";
RL Infect. Immun. 76:542-550(2008).
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; CP000766; ABY72411.1; -; Genomic_DNA.
DR RefSeq; WP_012150650.1; NC_010263.3.
DR AlphaFoldDB; B0BX35; -.
DR SMR; B0BX35; -.
DR STRING; 452659.RrIowa_0535; -.
DR EnsemblBacteria; ABY72411; ABY72411; RrIowa_0535.
DR GeneID; 45539030; -.
DR KEGG; rrj:RrIowa_0535; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_1_5; -.
DR OMA; PHWRFKL; -.
DR Proteomes; UP000000796; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00808; GluRS_core; 1.
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; IPR033910; GluRS_core.
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..447
FT /note="Glutamate--tRNA ligase 1"
FT /id="PRO_0000367760"
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 447 AA; 51700 MW; 1940C76543C4F711 CRC64;
MTKVITRFAP SPTGMLHVGN IRAALLNWLY AKKHNGQFIL RFDDTDLERS KQEYKDAIEE
DLKFLNINWD QTFNQLSRLS RYDAIKNLLL DKKRLYACYE TPEELELKRK FQLSKGLPPI
YDRASLNLTE EQAKKYIEQG RKPHYRFLVN HEPISWHDMI KGEVKYDGKA LSDPIVIRAD
GSMTYMLCSV IDDIDYDITH IIRGEDHVSN TAIQMQMFEA LNTTPPTFGH LSLIINKDEK
ISKRVGGFEI ATLRKEIGIE AMAIASFFSL LGSSAQILPY KSMEKLANQF EISSFSKSPT
IYQPEDLERL NHKLLISLDF DTVKERLKEI DAEYIDENFW LSVSPNLQKL RDVKDWWEIC
HQTPNVENLN LDKEYLKQAA ELLPKGEITK DSWSIWTKEI TNITGRKGKE LFLPLRLALT
ARESGPEIAS VLPLIDREEI IKRLTSA
