ID   SYM_MYCPN               Reviewed;         512 AA.
AC   P75091;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=MPN_023; ORFNames=MP131;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=11271496;
RX   DOI=10.1002/1522-2683(200011)21:17<3765::aid-elps3765>3.0.co;2-6;
RA   Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R.,
RA   Frank R.;
RT   "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL   Electrophoresis 21:3765-3780(2000).
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 2A subfamily. {ECO:0000305}.
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DR   EMBL; U00089; AAB95779.1; -; Genomic_DNA.
DR   PIR; S73457; S73457.
DR   RefSeq; NP_109711.1; NC_000912.1.
DR   RefSeq; WP_010874380.1; NC_000912.1.
DR   AlphaFoldDB; P75091; -.
DR   SMR; P75091; -.
DR   IntAct; P75091; 9.
DR   STRING; 272634.MPN_023; -.
DR   EnsemblBacteria; AAB95779; AAB95779; MPN_023.
DR   KEGG; mpn:MPN_023; -.
DR   PATRIC; fig|272634.6.peg.22; -.
DR   HOGENOM; CLU_009710_9_2_14; -.
DR   OMA; SDMHGTP; -.
DR   BioCyc; MPNE272634:G1GJ3-34-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
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; PF09334; tRNA-synt_1g; 2.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..512
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139229"
FT   MOTIF           11..21
FT                   /note="'HIGH' region"
FT   MOTIF           301..305
FT                   /note="'KMSKS' region"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   512 AA;  59263 MW;  B5C3861CEC30A6AA CRC64;
     MKRCYITTPI YYASGKPHIG HAFTTILADV IKRYKQQNGY EAYFLTGTDE HGNKIESKAK
     SLGLDPQTFV DQNVAYFQQM WKQLDINFDH FIRTTDLSHK AQVQHAFQLL YDKGLIYQSN
     WEGAYCVECE QNYFTYDKQT MLCEIGHQLT LVQEPSLFIA FKDSKDWIGE MIATNKLNIT
     PESRAAELKN NFLDGGLNDL ALTRQNVTWG IPVPFDNKQT IYVWFDALFN YITNLGFAHN
     DPKFNKWWNN NDEEHEVIHL ISREITRFHC IYWPIFLHQL GFKLPTQFLS HGWIVDGNGH
     KMSKSLGNVI SPEELLAQFG VDGTRYCLLK EMRLDKDNRC SMAIFKDIYN ADLANSFGNH
     ASRTFGMIKK YLGGQLDFIE VQDPQVKQLM DQANQAMVQF DTAWNNFQFY KGINGLLQLV
     FQASKLIDQL KPWELVKQTD YTLLKQLLFA CVRCTQVCFV LLAPILVHTS TQIFDLFNFS
     AQARSKTHLA DPQQLQKISL APVIQPLFKR LD