ID SYE2_ORITB Reviewed; 448 AA.
AC A5CFB7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 24-JAN-2024, entry version 84.
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=OTBS_1957;
OS Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=357244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boryong;
RX PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT "The Orientia tsutsugamushi genome reveals massive proliferation of
RT conjugative type IV secretion system and host-cell interaction genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAM81052.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM494475; CAM81052.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041621553.1; NC_009488.1.
DR AlphaFoldDB; A5CFB7; -.
DR SMR; A5CFB7; -.
DR KEGG; ots:OTBS_1957; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_1_5; -.
DR Proteomes; UP000001565; 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; HUPs; 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 NCBIfam; TIGR00464; gltX_bact; 1.
DR PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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..448
FT /note="Glutamate--tRNA ligase 2"
FT /id="PRO_0000367726"
FT MOTIF 9..19
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 448 AA; 51389 MW; 27F3179D43E053A6 CRC64;
MTVITRFAPS PTGKLHIGNV RVALVNWLYA QKYNGNFILR IDDTDRDRSK VEYHEAIIKD
LQWLGINWNS SFLQSIRFNK YKAAKQYLIS SGRLYECYET PEMLEIERKR QLTSGYPPIY
SRKALELTKA QKVQLQAEGY KVHYRFLIDR NKPIIWNDLI KGEIKYDGSN ISDPIVIKED
GTMIYMLCSV IDDIEYRISH IIRGEDHITN TAIQIQMFEA LGAAIPQLGH LSLIKSDSGK
ISKRIGGFTI DYLRDQLGIE PMAVNNLLAL SGTSNNVDAY FSLESLITKF DLSAFSKSAI
IYNENELVTL NHKLLVNTEY DTIKHRLTAI GLPDVTKEFW LAVRHNLNTL NDIKIWWQIC
YLPTLDKFQE QDAEFLKLAA GLLPSGKLTD NSWDDWVQNI IKATNRRGKA LFMPLRLALT
GITYGPELKY LLPLIGGEEV KARLLRHQ
//
