SYM_STRP1
ID SYM_STRP1 Reviewed; 665 AA.
AC Q9A178; Q490K5;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
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=SPy_0422, M5005_Spy0345;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK33446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004092; AAK33446.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000017; AAZ50963.1; -; Genomic_DNA.
DR RefSeq; NP_268725.1; NC_002737.2.
DR AlphaFoldDB; Q9A178; -.
DR SMR; Q9A178; -.
DR STRING; 1314.HKU360_00380; -.
DR PaxDb; Q9A178; -.
DR EnsemblBacteria; AAK33446; AAK33446; SPy_0422.
DR KEGG; spy:SPy_0422; -.
DR KEGG; spz:M5005_Spy0345; -.
DR PATRIC; fig|160490.10.peg.357; -.
DR HOGENOM; CLU_009710_9_4_9; -.
DR OMA; SDMHGTP; -.
DR Proteomes; UP000000750; 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..665
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139252"
FT DOMAIN 562..665
FT /note="tRNA-binding"
FT MOTIF 12..22
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 665 AA; 75131 MW; 34BE826F6A8639A1 CRC64;
MKKPFYITTP IYYPSGKLHI GSAYTTIACD VLARYKRLMG HEVFYLTGLD EHGQKIQTKA
KEAGITPQTY VDNMAKDVKA LWQLLDISYD TFIRTTDDYH EEVVAAVFEK LLAQDDIYLG
EYSGWYSVSD EEFFTESQLK EVFRDEDGQV IGGIAPSGHE VEWVSEESYF LRLSKYDDRL
VAFFKERPDF IQPDGRMNEM VKNFIEPGLE DLAVSRTTFT WGVPVPSDPK HVVYVWIDAL
LNYATALGYR QANHANFDKF WNGTVFHMVG KDILRFHSIY WPILLMMLDL PMPDRLIAHG
WFVMKDGKMS KSKGNVVYPE MLVERFGLDP LRYYLMRSLP VGSDGTFTPE DYVGRINYEL
ANDLGNLLNR TVAMINKYFD GTVPAYVDNG TAFDADLSQL IDAQLADYHK HMEAVDYPRA
LEAVWTIIAR TNKYIDETAP WVLAKEDGDK AQLASVMAHL AASLRLVAHV IQPFMMETSA
AIMAQLGLEP VSDLSTLALA DFPANTKVVA KGTPIFPRLD MEAEIDYIKA QMGDSSAISQ
EKEWVPEEVA LKSEKDVITF ETFDAVEIRV AEVKEVSKVE GSEKLLRFRV DAGDGQDRQI
LSGIAKFYPN EQELVGKKLQ IVANLKPRKM MKKYISQGMI LSAEHGDQLT VLTVDSSVPN
GSIIG
