ID   SYM_STAAW               Reviewed;         657 AA.
AC   Q8NY00;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01228};
DE            EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_01228};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01228};
DE            Short=MetRS {ECO:0000255|HAMAP-Rule:MF_01228};
GN   Name=metG {ECO:0000255|HAMAP-Rule:MF_01228}; Synonyms=metS;
GN   OrderedLocusNames=MW0445;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(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:0000255|HAMAP-Rule:MF_01228}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01228};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01228}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2B subfamily. {ECO:0000255|HAMAP-Rule:MF_01228}.
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DR   EMBL; BA000033; BAB94310.1; -; Genomic_DNA.
DR   RefSeq; WP_001051130.1; NC_003923.1.
DR   AlphaFoldDB; Q8NY00; -.
DR   SMR; Q8NY00; -.
DR   BindingDB; Q8NY00; -.
DR   ChEMBL; CHEMBL5372; -.
DR   EnsemblBacteria; BAB94310; BAB94310; BAB94310.
DR   KEGG; sam:MW0445; -.
DR   HOGENOM; CLU_009710_9_4_9; -.
DR   OMA; SDMHGTP; -.
DR   Proteomes; UP000000418; 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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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   CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR   Gene3D; 2.40.50.140; -; 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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR004495; Met-tRNA-synth_bsu_C.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43326; PTHR43326; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding.
FT   CHAIN           1..657
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139244"
FT   DOMAIN          557..657
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT   MOTIF           13..23
FT                   /note="'HIGH' region"
FT   MOTIF           308..312
FT                   /note="'KMSKS' region"
FT   BINDING         311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   657 AA;  74872 MW;  12C96E35EFB3D01A CRC64;
     MAKETFYITT PIYYPSGNLH IGHAYSTVAG DVIARYKRMQ GYDVRYLTGT DEHGQKIQEK
     AQKAGKTEIE YLDEMIAGIK QLWAKLEISN DDFIRTTEER HKHVVEQVFE RLLKQGDIYL
     GEYEGWYSVP DETYYTESQL VDPQYENGKI IGGKSPDSGH EVELVKEESY FFNISKYTDR
     LLEFYDQNPD FIQPPSRKNE MINNFIKPGL ADLAVSRTSF NWGVHVPSNP KHVVYVWIDA
     LVNYISALGY LSDDESLFNK YWPADIHLMA KEIVRFHSII WPILLMALDL PLPKKVFAHG
     WILMKDGKMS KSKGNVVDPN ILIDRYGLDA TRYYLMRELP FGSDGVFTPE AFVERTNFDL
     ANDLGNLVNR TISMVNKYFD GELPAYQGPL HELDEEMEAM ALETVKSYTE SMESLQFSVA
     LSTVWKFISR TNKYIDETTP WVLAKDDSQK DMLGNVMAHL VENIRYAAVL LRPFLTHAPK
     EIFEQLNINN PQFMEFSSLE QYGVLTESIM VTGQPKPIFP RLDSEAEIAY IKESMQPPAT
     EEEKEEIPSK PQIDIKDFDK VEIKAATIIN AEHVKKSDKL LKIQVDLDSE QRQIVSGIAK
     FYTPDDIIGK KVAVVTNLKP AKLMGQKSEG MILSAEKDGV LTLVSLPSAI PNGAVIK