SYM_CAMJE
ID SYM_CAMJE Reviewed; 628 AA.
AC Q9PP85; Q0PA52;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=Cj0838c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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 2A subfamily. {ECO:0000305}.
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DR EMBL; AL111168; CAL34966.1; -; Genomic_DNA.
DR PIR; F81356; F81356.
DR RefSeq; WP_002852639.1; NC_002163.1.
DR RefSeq; YP_002344245.1; NC_002163.1.
DR AlphaFoldDB; Q9PP85; -.
DR SMR; Q9PP85; -.
DR IntAct; Q9PP85; 1.
DR STRING; 192222.Cj0838c; -.
DR PaxDb; Q9PP85; -.
DR PRIDE; Q9PP85; -.
DR EnsemblBacteria; CAL34966; CAL34966; Cj0838c.
DR GeneID; 905186; -.
DR KEGG; cje:Cj0838c; -.
DR PATRIC; fig|192222.6.peg.826; -.
DR eggNOG; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_4_7; -.
DR OMA; SDMHGTP; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; IPR002300; aa-tRNA-synth_Ia.
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; PF00133; tRNA-synt_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; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..628
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139214"
FT DOMAIN 527..628
FT /note="tRNA-binding"
FT MOTIF 9..19
FT /note="'HIGH' region"
FT MOTIF 294..298
FT /note="'KMSKS' region"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 628 AA; 72210 MW; 223511732F83663C CRC64;
MRYITTPIYY VNDVPHLGHA YTTIIADTLA RFYRLQGHET RFLTGTDEHG QKIEEAAKLR
NSTPQEYADK ISFEFKKLWD EFEITYDIYA RTTDTRHIEF IKAMFLKMWQ KGDIYKDEYE
GHYCISCESF FTQSQLINDC SCPDCGKQTR ILKEESYFFK LSKYQDKILQ WYEEKDPILP
KNKKNELINF VQNGLKDLSI TRTSFDWGIK LPQEINDDKH IIYVWLDALF IYVSSLDFQN
KGENAKFWPA HVHLVGKDIL RFHAIYWPAF LMSVDLPLPK FIGAHGWWTK EGEKMSKSKG
NVVKPKEVVD AYGSEAFRYF LLREVPFGND GDFSENMLIN RINAELSNEF GNLLNRIIGM
STKYSQGNIS KEGVLKFYNA ELNQAKEHLN LAVEFLENLQ CNRYLEELFK ALSVANLAIS
KYEPWSLIKE NKHEQANALV ALCANILAKT SLLLSPTLPK SSQKVALALN FEISSANYTK
MILDNELLDF KANPCEALFP KVEKALLKQE IKEEPKKEES PKIKIDDFAK IEIKVAKVLD
CQNIEGSEKL LKFQLELDDK EIRQVLSGIA KYYKASDLIG KQVCVISNLK KAKIFGHESD
GMILSAKSGD KLVLIAPEQL VQNGSLVG
