ID   SYM_LISMO               Reviewed;         664 AA.
AC   Q8YAF2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, 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=lmo0177;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(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; AL591973; CAC98392.1; -; Genomic_DNA.
DR   PIR; AB1097; AB1097.
DR   RefSeq; NP_463708.1; NC_003210.1.
DR   RefSeq; WP_003733137.1; NC_003210.1.
DR   AlphaFoldDB; Q8YAF2; -.
DR   SMR; Q8YAF2; -.
DR   STRING; 169963.lmo0177; -.
DR   PaxDb; Q8YAF2; -.
DR   EnsemblBacteria; CAC98392; CAC98392; CAC98392.
DR   GeneID; 986940; -.
DR   KEGG; lmo:lmo0177; -.
DR   PATRIC; fig|169963.11.peg.182; -.
DR   eggNOG; COG0073; Bacteria.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_4_9; -.
DR   OMA; SDMHGTP; -.
DR   PhylomeDB; Q8YAF2; -.
DR   BioCyc; LMON169963:LMO0177-MON; -.
DR   Proteomes; UP000000817; 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; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
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..664
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139227"
FT   DOMAIN          563..664
FT                   /note="tRNA-binding"
FT   MOTIF           15..25
FT                   /note="'HIGH' region"
FT   MOTIF           310..314
FT                   /note="'KMSKS' region"
FT   BINDING         313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   664 AA;  75651 MW;  1A1AC2A90D8BF351 CRC64;
     MPEEKNTFYI TTPIYYPSGK AHIGHAYTTV AGDAMARYKR LKGYDVFYLT GTDEHGQKIQ
     AKAKERGISE QEYVDEIAEG FQELWKKLEI SNTDFIRTTQ DRHKTSVEKI FEQLLEQGDI
     YLGEYEGWYS VSDEEYFTET QLEEVYKDEN GKVIGGKAPS GNEVELVKEE SYFFRMSKYA
     DRLVEYYNSH PEFILPESRK NEMINNFIKP GLEDLAVSRT TFDWGIKVPG NPKHVVYVWI
     DALSNYITAL GYNTDNDTKF QKYWPADVQI VGKEIVRFHT IYWPIMLMAL DLPLPKMVFG
     HGWILMKDGK MSKSKGNVVD PYMLIDRYGL DALRYYLLRE VPFGSDGLFT PEDFVDRVNF
     DLANDLGNLL NRTVAMINKY FDGEIPAYQG NVTEFDQILV DFKNNVVKEY EGSMDHMQFS
     VALNQLWSLI SRTNKYIDET APWALAKDED KRTELASVMT HLAENLRIIA VLLQPFLTRT
     PGEIFLQLGL QEENLKKWDS IYGYGEIPAG TTVVKKGTPI FPRLDAEVEV TYIQDEMKGS
     APAPAEEVAE VEALETPQIG IEDFDKIDLR VAEVKQVDKV KKADKLLCFQ LDLGEGKLRQ
     VLSGIAEFYQ PEELIGKKVI VVSNLKPVKL RGLMSEGMIL SGEKDGKLSV IEASSALPNG
     AKVK