ID   SYM_BRUME               Reviewed;         515 AA.
AC   Q8YH17;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 119.
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}; OrderedLocusNames=BMEI0987;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(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: Monomer. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL52168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL52168.1; ALT_INIT; Genomic_DNA.
DR   PIR; AE3375; AE3375.
DR   RefSeq; WP_004683748.1; NZ_GG703778.1.
DR   AlphaFoldDB; Q8YH17; -.
DR   SMR; Q8YH17; -.
DR   STRING; 224914.BMEI0987; -.
DR   EnsemblBacteria; AAL52168; AAL52168; BMEI0987.
DR   GeneID; 29593805; -.
DR   KEGG; bme:BMEI0987; -.
DR   PATRIC; fig|224914.52.peg.452; -.
DR   eggNOG; COG0143; Bacteria.
DR   OMA; SDMHGTP; -.
DR   PhylomeDB; Q8YH17; -.
DR   Proteomes; UP000000419; Chromosome I.
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; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
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.
FT   CHAIN           1..515
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139212"
FT   MOTIF           13..23
FT                   /note="'HIGH' region"
FT   MOTIF           300..304
FT                   /note="'KMSKS' region"
FT   BINDING         303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   515 AA;  57998 MW;  670735824F92AF00 CRC64;
     MSREKYYITT AIAYPNGKPH IGHAYELIAT DAMARFQRLN GMDVYFLTGT DEHGIKMLQS
     ARKEGITPRE LADRNTSAFR RMAEVLNSSN DDYIRTSEER HYKASQVIWQ AMVANGDIYK
     GGYAGWYSVR DEAYYGEEET EVRADGVRYG PQGTPVEWVE EESYFFRLSA YQDKLLDLYE
     NNPGFIMPAE RRNEIVSFVK SGLKDLSISR TTFDWGIPVP GDEKHVMYVW VDALTNYITA
     LGYPDTTDER WAYWPANAHI IGKDISRFHA VYWPAFLMSA QLPLPKRVFA HGFLFNRGEK
     MSKSVGNVID PFELVERYGL DQLRYFLMRE VPFGQDGSYS HEAIVNRTNA DLANDLGNLA
     QRSLSMIAKN CEGKVPQPGA FSEADKAILD QADAALETAR KAMDDQALHL ALGAIFAVVA
     EANRYFAGQE PWALRKTDPA RMGTVLYVTA EVLRRVGIMV QPFIPQSAEK LLDILAAPAD
     KRQFADVLAS PLAGGTDLPA PQPVFPRYVE ADEQN