ID SYM_LISMF Reviewed; 665 AA.
AC Q724N6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
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};
GN OrderedLocusNames=LMOf2365_0188;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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: Homodimer. {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}.
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DR EMBL; AE017262; AAT02975.1; -; Genomic_DNA.
DR AlphaFoldDB; Q724N6; -.
DR SMR; Q724N6; -.
DR KEGG; lmf:LMOf2365_0188; -.
DR HOGENOM; CLU_009710_9_4_9; -.
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; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 NCBIfam; TIGR00398; metG; 1.
DR NCBIfam; TIGR00399; metG_C_term; 1.
DR PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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_0000139226"
FT DOMAIN 564..665
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT MOTIF 16..26
FT /note="'HIGH' region"
FT MOTIF 311..315
FT /note="'KMSKS' region"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
SQ SEQUENCE 665 AA; 75767 MW; B4FCE15778689C27 CRC64;
MLPEEKNTFY ITTPIYYPSG KAHIGHAYTT VAGDAMARYK RLKGYDVFYL TGTDEHGQKI
QAKAKERGIS EQEYVDEIAE GFQELWKKLE ISNTDFIRTT QDRHKTSVEK IFEQLLEQGD
IYLGEYEGWY SVSDEEYFTE TQLEEVYKDE NGKVIGGKAP SGNEVELVKE ESYFFRMSKY
ADRLVEYYNS HPEFILPESR KNEMINNFIK PGLEDLAVSR TTFDWGIKVP GNPKHVVYVW
IDALSNYITA LGYNTDNDTK FQKYWPADVQ IVGKEIVRFH TIYWPIMLMA LDLPLPKMVF
GHGWILMKDG KMSKSKGNVV DPYMLIDRYG LDALRYYLLR EVPFGSDGLF TPEDFVDRVN
FDLANDLGNL LNRTVAMINK YFDGEIPAYQ GNVTEFDQTL VDFKNNVVKE YEGSMDHMQF
SVALNQLWSL ISRTNKYIDE TAPWTLAKDE DKRTELASVM THLAENLRII AVLLQPFLTR
TPGEIFLQLG LQEENLKKWD SIYGYGEIPA GTTVVKKGTP IFPRLEAEVE VTYIQDEMKG
SAPAPAKEAA EVEALETPQI GIEDFDKIDL RVAEVKQVDK VKKADKLLCF QLDLGEGKLR
QVLSGIAEFY QPEELIGKKV IVVSNLKPVK LRGLMSEGMI LSGEKDGKLS VIEASSALPN
GAKVK
//
