SYM_CHLTR
ID SYM_CHLTR Reviewed; 550 AA.
AC O84035;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Methionine--tRNA ligase;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=metG; OrderedLocusNames=CT_032;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
CC -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC also for the initiation of all mRNA translation through initiator
CC tRNA(fMet) aminoacylation. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 1 subfamily. {ECO:0000305}.
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DR EMBL; AE001273; AAC67622.1; -; Genomic_DNA.
DR PIR; C71567; C71567.
DR RefSeq; NP_219534.1; NC_000117.1.
DR RefSeq; WP_010724990.1; NC_000117.1.
DR AlphaFoldDB; O84035; -.
DR SMR; O84035; -.
DR STRING; 813.O172_00170; -.
DR EnsemblBacteria; AAC67622; AAC67622; CT_032.
DR GeneID; 884148; -.
DR KEGG; ctr:CT_032; -.
DR PATRIC; fig|272561.5.peg.37; -.
DR HOGENOM; CLU_009710_1_2_0; -.
DR InParanoid; O84035; -.
DR OMA; SDMHGTP; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR45765; PTHR45765; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF57770; SSF57770; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..550
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139123"
FT MOTIF 13..23
FT /note="'HIGH' region"
FT MOTIF 331..335
FT /note="'KMSKS' region"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 62716 MW; B829F13C23D5E9C5 CRC64;
MESSRILITS ALPYANGPLH FGHITGAYLP ADVYARFQRL QGKEVLYICG SDEYGIAITL
NAELAGMGYQ EYVDMYHKLH KDTFKKLGIS VDFFSRTTNT YHPAIVQDFY RNLQERGLVE
NQVTEQLYSE EEGKFLADRY VVGTCPKCGF DRARGDECQQ CGADYEARDL KEPRSKLTGA
ALSLRDTEHA YLHLERMKED LLAFVQGIYL RPHMRNFVTD YIEHLRPRAV TRDLSWGIPV
PDLENKVFYV WFDAPIGYIS GTMDWAASIG DPEAWKKFWL DDTVTYAQFI GKDNTSFHAA
IFPAMEIGQS LPYKKVDALV TSEFLLLEGF QFSKSDGNFI DMDAFLETYS LDKLRYVLAA
IAPETSDSEF SFQEFKTRCN SELVGKYGNF VNRVLAFAVK NGCTELSSPQ LEQKDLDFIS
KSQKLAKDAA EHYAQYSLRK ACSTIMELAA LGNGYFNDEA PWKLAKEGNW NRVRAILFCA
CYCQKLLALI SYPIMPETAL KILEMIAPHS LDLGSQDPDR LQSLWTDSFF DYSEEKFSLK
EPELLFTMVE