ID   SYM_MYCTO               Reviewed;         519 AA.
AC   P9WFU4; L0T8C8; O05593;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=metG; Synonyms=metS; OrderedLocusNames=MT1036;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2B subfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45286.1; -; Genomic_DNA.
DR   PIR; B70603; B70603.
DR   RefSeq; WP_003405183.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFU4; -.
DR   SMR; P9WFU4; -.
DR   EnsemblBacteria; AAK45286; AAK45286; MT1036.
DR   GeneID; 45424979; -.
DR   KEGG; mtc:MT1036; -.
DR   PATRIC; fig|83331.31.peg.1111; -.
DR   HOGENOM; CLU_009710_9_4_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43326; PTHR43326; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00398; metG; 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..519
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000428476"
FT   REGION          500..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           11..21
FT                   /note="'HIGH' region"
FT   MOTIF           299..303
FT                   /note="'KMSKS' region"
FT   COMPBIAS        501..519
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   519 AA;  57994 MW;  FC019248902EE6E2 CRC64;
     MKPYYVTTAI AYPNAAPHVG HAYEYIATDA IARFKRLDGY DVRFLTGTDE HGLKVAQAAA
     AAGVPTAALA RRNSDVFQRM QEALNISFDR FIRTTDADHH EASKELWRRM SAAGDIYLDN
     YSGWYSVRDE RFFVESETQL VDGTRLTVET GTPVTWTEEQ TYFFRLSAYT DKLLAHYHAN
     PDFIAPETRR NEVISFVSGG LDDLSISRTS FDWGVQVPEH PDHVMYVWVD ALTNYLTGAG
     FPDTDSELFR RYWPADLHMI GKDIIRFHAV YWPAFLMSAG IELPRRIFAH GFLHNRGEKM
     SKSVGNIVDP VALAEALGVD QVRYFLLREV PFGQDGSYSD EAIVTRINTD LANELGNLAQ
     RSLSMVAKNL DGRVPNPGEF ADADAALLAT ADGLLERVRG HFDAQAMHLA LEAIWLMLGD
     ANKYFSVQQP WVLRKSESEA DQARFRTTLY VTCEVVRIAA LLIQPVMPES AGKILDLLGQ
     APNQRSFAAV GVRLTPGTAL PPPTGVFPRY QPPQPPEGK