SYM_STAES
ID SYM_STAES Reviewed; 656 AA.
AC Q8CQU3;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=SE_2293;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05935.1; -; Genomic_DNA.
DR RefSeq; NP_765848.1; NC_004461.1.
DR RefSeq; WP_002457101.1; NZ_WBME01000023.1.
DR AlphaFoldDB; Q8CQU3; -.
DR SMR; Q8CQU3; -.
DR STRING; 176280.SE_2293; -.
DR EnsemblBacteria; AAO05935; AAO05935; SE_2293.
DR GeneID; 50019599; -.
DR KEGG; sep:SE_2293; -.
DR PATRIC; fig|176280.10.peg.2236; -.
DR eggNOG; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_4_9; -.
DR OMA; SDMHGTP; -.
DR Proteomes; UP000001411; 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; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 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; PS00178; AA_TRNA_LIGASE_I; 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..656
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139245"
FT DOMAIN 556..656
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT MOTIF 13..23
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:0000255|HAMAP-Rule:MF_01228"
SQ SEQUENCE 656 AA; 75117 MW; E5F34D9D684239A1 CRC64;
MAKDTFYITT PIYYPSGNLH IGHAYSTVAG DVIARYKRMQ GYDVRYLTGT DEHGQKIQEK
AQKAGKTELE YLDEMISGIK NLWSKLEISN DDFIRTTEER HKQVVEKVFE RLLKQGDIYL
GEYEGWYSVP DETYYTESQL VDPVYENGKI VGGKSPDSGH EVELVKEESY FFNINKYTDR
LLEFYDENPD FIQPPSRKNE MINNFIKPGL EDLAVSRTSF DWGVRVPSNP KHVVYVWIDA
LVNYISSLGY LSDDETLFNK YWPADIHLMA KEIVRFHSII WPILLMALDL PLPKKVFAHG
WILMKDGKMS KSKGNVVDPN VLIDRYGLDA TRYYLMRELP FGSDGVFTPE AFVERTNYDL
ANDLGNLVNR TISMINKYFH GELPAYQGPK HELDEKMEAM ALETVKSFND NMESLQFSVA
LSTVWKFISR TNKYIDETQP WVLAKDENQR EMLGNVMAHL VENIRFATIL LQPFLTHAPR
EIFKQLNINN PDLHQLDSLQ QYGMLSEAIT VTEKPTPIFP RLDTEAEIAY IKESMQPPKS
IKQSDEPGKE QIDIKDFDKV EIKAATIIDA ENVKKSEKLL KIKVELDNEQ RQIVSGIAKF
YRPEDIIGKK VAVVTNLKPA KLMGQKSEGM ILSAEKDGVL TLISLPSAIP NGAVIK
