SYE_CHLP6
ID SYE_CHLP6 Reviewed; 505 AA.
AC P59691; F0T375; P94662; Q06560;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022};
DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022};
GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022};
GN OrderedLocusNames=CPSIT_0206, G5O_0208;
OS Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia psittaci).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=331636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-125 / 6BC;
RX PubMed=21441521; DOI=10.1128/jb.00236-11;
RA Voigt A., Schofl G., Heidrich A., Sachse K., Saluz H.P.;
RT "Full-length de novo sequence of the Chlamydophila psittaci type strain,
RT 6BC.";
RL J. Bacteriol. 193:2662-2663(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-125 / 6BC;
RX PubMed=21622741; DOI=10.1128/jb.05277-11;
RA Grinblat-Huse V., Drabek E.F., Creasy H.H., Daugherty S.C., Jones K.M.,
RA Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P., Bavoil P., Myers G.S.;
RT "Genome sequences of the zoonotic pathogens Chlamydia psittaci 6BC and
RT Cal10.";
RL J. Bacteriol. 193:4039-4040(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368.
RC STRAIN=ATCC VR-125 / 6BC;
RX PubMed=8491714; DOI=10.1128/jb.175.10.2936-2942.1993;
RA Wichlan D.W., Hatch T.P.;
RT "Identification of an early-stage gene of Chlamydia psittaci 6BC.";
RL J. Bacteriol. 175:2936-2942(1993).
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=AAA23122.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; CP002549; ADZ18786.1; -; Genomic_DNA.
DR EMBL; CP002586; AEB55211.1; -; Genomic_DNA.
DR EMBL; L13598; AAA23122.1; ALT_INIT; Genomic_DNA.
DR PIR; A36909; A36909.
DR RefSeq; WP_006342859.1; NC_017287.1.
DR AlphaFoldDB; P59691; -.
DR SMR; P59691; -.
DR GeneID; 12242467; -.
DR KEGG; chb:G5O_0208; -.
DR KEGG; chp:CPSIT_0206; -.
DR PATRIC; fig|331636.3.peg.193; -.
DR HOGENOM; CLU_015768_6_3_0; -.
DR OMA; WDEGPFF; -.
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..505
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119540"
FT MOTIF 12..22
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 253..257
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ SEQUENCE 505 AA; 58540 MW; 9D51E741448A9B22 CRC64;
MAWENVRVRV APSPTGDPHV GTAYMALFNE IFAKRFNGKM ILRIEDTDQT RSRDDYEKNI
FSALKWCGIQ WDEGPDIGGP YGPYRQSERT EIYREYAELL LKTDYAYKCF ATPKELEEMR
AVATTLGYRG GYDRRYRYLS PEEIEARTRE GQPYTIRLKV PLTGECVLDD YCKGRVVFPW
ADVDDQVLIK SDGFPTYHFA NVVDDHLMGI THVLRGEEWL SSTPKHLLLY EAFGWEAPTF
LHMPLLLNPD GTKLSKRKNP TSIFYYRDAG YVKEAFMNFL TLMGYSMEGD EEIYSLEKLI
ANFDPRRIGK SGAVFDTRKL DWMNKHYLTH EKSSESLLAK LKDWLINDEF FLKILPLCQS
RITTLAEFIG FTGFFFSVLP EYSKEELLPA TIVEEKAAIL LYSYVKYLEK ADLWVKDQFY
QGSKWLSSAF QVHHKKVVIP LLYVAITGKK QGLPLFDSME LLGKPRTRAR LVHAQNLLGG
VPKKIQTTID KVLKEEDFEN KIFEF
