ID   SYM_MYCPU               Reviewed;         509 AA.
AC   Q50319;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 131.
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=MYPU_4900;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-281.
RC   STRAIN=KD735-16;
RX   PubMed=8636032; DOI=10.1128/jb.178.8.2314-2319.1996;
RA   Wang X., Lutkenhaus J.;
RT   "Characterization of the ftsZ gene from Mycoplasma pulmonis, an organism
RT   lacking a cell wall.";
RL   J. Bacteriol. 178:2314-2319(1996).
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; AL445564; CAC13663.1; -; Genomic_DNA.
DR   EMBL; U34931; AAC44094.1; -; Genomic_DNA.
DR   PIR; B90573; B90573.
DR   PIR; PC6005; PC6005.
DR   RefSeq; WP_010925291.1; NC_002771.1.
DR   AlphaFoldDB; Q50319; -.
DR   SMR; Q50319; -.
DR   STRING; 272635.MYPU_4900; -.
DR   PRIDE; Q50319; -.
DR   EnsemblBacteria; CAC13663; CAC13663; CAC13663.
DR   KEGG; mpu:MYPU_4900; -.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_4_14; -.
DR   OMA; SDMHGTP; -.
DR   OrthoDB; 761140at2; -.
DR   BioCyc; MPUL272635:G1GT6-494-MON; -.
DR   Proteomes; UP000000528; 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; 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; Reference proteome.
FT   CHAIN           1..509
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139230"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT   MOTIF           302..306
FT                   /note="'KMSKS' region"
FT   BINDING         305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        215
FT                   /note="I -> M (in Ref. 2; AAC44094)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   509 AA;  59892 MW;  D047D1EC30F80B56 CRC64;
     MKKTIYITTP IYYPSGDLHL GHIYSTNIAW VLRNYKKIQG YETFFSTGSD EHGQKIFNKA
     QELKLETQDY VDRQANKFID FWKKANIDYD FFARTTNKEH KEVVREIFHK LKEKNIIYLD
     KYVGLYSVSD EEFLTETQAL KKDNKFFHPV SNHELIKIEE ESYFFNLNLF IDWIKEFLDQ
     DIISSKAIVN ELKSNFINKG LENLSVTRIK LDWGIKIDQS SKHVIYVWLD ALFQYLTNLG
     YGSKNQSLYE KFWKNGDERV HVVGKEITRF HCIYWPIFLK SLNVKMPTKI ISHGWIVTPE
     GKMSKSKGNV VDPVVLIEKY GSEVLKYFLI AKLSIKKDGV FSEELLVSAY NNDLVNTFSN
     LISRTVKMIL NNYDRPLSFI LSKDQEDLEI EKDIKNSFET FCSFAEEYEF DKAFESTINL
     GKKLNLYIDK TRPWLLTKED QKLEIVLNRL LNGIYAMAFE LSIVMPQTSQ KLAKALGFES
     FEKSKLEDFK KFDNIKIEKI ENLFNRIKL