ID   SYM_LACLA               Reviewed;         662 AA.
AC   Q9CHE0;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=LL0792; ORFNames=L0353;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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: Homodimer. {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; AE005176; AAK04890.1; -; Genomic_DNA.
DR   PIR; H86723; H86723.
DR   RefSeq; NP_266948.1; NC_002662.1.
DR   RefSeq; WP_010905562.1; NC_002662.1.
DR   AlphaFoldDB; Q9CHE0; -.
DR   SMR; Q9CHE0; -.
DR   STRING; 272623.L0353; -.
DR   PaxDb; Q9CHE0; -.
DR   EnsemblBacteria; AAK04890; AAK04890; L0353.
DR   KEGG; lla:L0353; -.
DR   PATRIC; fig|272623.7.peg.847; -.
DR   eggNOG; COG0073; Bacteria.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_4_9; -.
DR   OMA; SDMHGTP; -.
DR   Proteomes; UP000002196; 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; IPR041872; Anticodon_Met.
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; PF19303; Anticodon_3; 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; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..662
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139223"
FT   DOMAIN          559..662
FT                   /note="tRNA-binding"
FT   MOTIF           14..24
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:0000250"
SQ   SEQUENCE   662 AA;  75777 MW;  5538AAAD66F1CB91 CRC64;
     MTENKTFYIT TPIYYPSGKL HLGSSYTTIA CDVLARYKRL MGFDTFYLTG LDEHGMKIQR
     KAEELGMTPK EYLDPMAADV QELWKKLDIS YDKFIRTTDT YHEEAVAKAF EQLLEQDDIY
     LGKYAGWYSV SDEEFFTETQ LEEIFRDESG NITGGIAPSG HEVEWVEEET YFFRMGKYAD
     WLLQYYDEHP DFIQPEVRKN EMVNNFIKPG LEDLALTRTS FTWGIPVPSN PKHVVYVWFD
     ALLNYITALG YNSDNDSNFK KYWPGINMVG KEIVRFHTIY WPIMLHALGL PAPKKIFAHG
     WLLMKDGKMS KSKGNVVYPE MLIERYGLDA VRYYLMRAIS FGQDGIFTPE DFVGRINFDL
     ANDLGNLLNR TVSMINKYND GKIEATGVST EFDASLEEVV EETISHFHKA MDKFEFNVAL
     ADVWTLISRT NKYIDETAPW VLAKSEDDKA KLNNVLYHLA ENLRIAGALL QPFMRATSGK
     IFEQLGMDER SFSLENLSFG YSFTHPVVAK GQPIFPRLDV EEEVAYIKLQ MAGGVLPEKE
     WVPEEVELNL TLPQIKFDDF EKIELKVAEV LEVEPVEGSD KLLRFKLDAG DSEPRQILSG
     IAQFYPNEQE LVGKKLQIVA NLKPRKMMKK YVSQGMILSA EFDGKLSVLT VDDDVPAGSL
     IG