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   24-JUL-2024, entry version 133.
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 serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-885 / DSM 19411 / 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; 272561.CT_032; -.
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   OrthoDB; 9810191at2; -.
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; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 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   NCBIfam; TIGR00398; metG; 1.
DR   PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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
//