ID   SYM_STRPN               Reviewed;         665 AA.
AC   P67580; Q97RL6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=SP_0788;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(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; AE005672; AAK74925.1; -; Genomic_DNA.
DR   PIR; D95091; D95091.
DR   RefSeq; WP_001291370.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P67580; -.
DR   SMR; P67580; -.
DR   STRING; 170187.SP_0788; -.
DR   PRIDE; P67580; -.
DR   EnsemblBacteria; AAK74925; AAK74925; SP_0788.
DR   GeneID; 60234114; -.
DR   KEGG; spn:SP_0788; -.
DR   eggNOG; COG0073; Bacteria.
DR   eggNOG; COG0143; Bacteria.
DR   OMA; SDMHGTP; -.
DR   PhylomeDB; P67580; -.
DR   BioCyc; SPNE170187:G1FZB-805-MON; -.
DR   Proteomes; UP000000585; 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; RNA-binding; tRNA-binding.
FT   CHAIN           1..665
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139250"
FT   DOMAIN          562..665
FT                   /note="tRNA-binding"
FT   MOTIF           13..23
FT                   /note="'HIGH' region"
FT   MOTIF           309..313
FT                   /note="'KMSKS' region"
FT   BINDING         312
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   665 AA;  75651 MW;  7FAB60A5CC49A56D CRC64;
     MSEKNFYITT PIYYPSGKLH IGSAYTTIAC DVLARYKRLM GYDVFYLTGL DEHGQKIQQK
     AEEAGITPQA YVDGMAVGVK ELWQLLDISY DKFIRTTDDY HEKVVAQVFE RLLAQDDIYL
     GEYSGWYSVS DEEFFTESQL AEVFRDEAGN VTGGIAPSGH EVEWVSEESY FLRLSKYQDR
     LVEFFKAHPE FITPDGRLNE MLRNFIEPGL EDLAVSRTTF TWGVPVPSNP KHVVYVWIDA
     LLNYATALGY AQDEHGNFDK FWNGTVFHMV GKDILRFHSI YWPILLMMLD VKLPDRLIAH
     GWFVMKDGKM SKSKGNVVYP EMLVERYGLD PLRYYLMRNL PVGSDGTFTP EDYVGRINYE
     LANDLGNLLN RTVSMINKYF DGQIPAYVEG VTEFDHVLAE VAEQSIADFH THMEAVDYPR
     ALEAVWTLIS RTNKYIDETA PWVLAKDEAL RDQLASVMSH LAASIRVVAH LIEPFMMETS
     RAVLTQLGLE EVSSLENLSL ADFPADVTVV AKGTPIFPRL NMEEEIAYIK EQMEGNKPAV
     EKEWNPDEVE LKLNKDEIKF EDFDKVEIRV AEVKEVSKVE GSDKLLQFRL DAGDGEDRQI
     LSGIAKYYPN EQELVGKKVQ IVANLKPRKM MKKYVSQGMI LSAEHDGKLT LLTVDPAVPN
     GSVIG