ID   SYM_HELPY               Reviewed;         650 AA.
AC   P56127;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=metG; OrderedLocusNames=HP_0417;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000511; AAD07483.1; -; Genomic_DNA.
DR   PIR; A64572; A64572.
DR   RefSeq; NP_207215.1; NC_000915.1.
DR   RefSeq; WP_001172573.1; NC_018939.1.
DR   AlphaFoldDB; P56127; -.
DR   SMR; P56127; -.
DR   DIP; DIP-3541N; -.
DR   IntAct; P56127; 1.
DR   MINT; P56127; -.
DR   STRING; 85962.HP_0417; -.
DR   PaxDb; 85962-C694_02125; -.
DR   EnsemblBacteria; AAD07483; AAD07483; HP_0417.
DR   KEGG; hpy:HP_0417; -.
DR   PATRIC; fig|85962.47.peg.442; -.
DR   eggNOG; COG0073; Bacteria.
DR   eggNOG; COG0143; Bacteria.
DR   InParanoid; P56127; -.
DR   OrthoDB; 9810191at2; -.
DR   PhylomeDB; P56127; -.
DR   Proteomes; UP000000429; 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; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
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; 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; 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; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding; Zinc.
FT   CHAIN           1..650
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139221"
FT   DOMAIN          549..650
FT                   /note="tRNA-binding"
FT   REGION          513..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           11..21
FT                   /note="'HIGH' region"
FT   MOTIF           301..305
FT                   /note="'KMSKS' region"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   650 AA;  74507 MW;  CEFDF457B9F75DD3 CRC64;
     MQKSLITTPI YYVNDIPHIG HAYTTLIADT LKKYYTLQGE EVFFLTGTDE HGQKIEQSAR
     LRNQSPKAYA DSISTIFKDQ WDFFNLDYDG FIRTTDSEHQ KCVQNAFEIM FEKGDIYKGA
     YSGYYCVSCE SYCAISKADN TNDKVLCPDC LRETTLLEEE SYFFRLSAYE KPLLDFYAKN
     PEAILPVYRK NEVTSFIEQG LLDLSITRTS FEWGIPLPKK MNDPKHVVYV WLDALLNYAS
     ALGYLNDLDN KMAHFECARH IVGKDILRFH AIYWPAFLMS LNLPLFKQLC VHGWWTIEGV
     KMSKSLGNVL DAQKIAMEYG IEELRYFLLR EVPFGQDGDF SKKALIERIN ANLNNDLGNL
     LNRLLGMAKK YFNHSLKSTK ITAYYSKELE KVHQILDNAN SFVPKMQLHK ALEELFNVYD
     FLNKLIAKEE PWVLHKNNES EKLEALLSLI ANALLQSSFL LYAFMPKSAV KLANAFNTEI
     TPDNYERFFK AKKLQDMILQ DTEPLFSKME KIEKTEKAGE ASPEKNEKEK KDAKEKAPLK
     QENYIGIEDF KKVEIKVGLI KEAQRIEKSN KLLRLKVDLG EGRLRQIISG IALDYEPESL
     VGQMVCVVAN LKPAKLMGEM SEGMILAVRD SDNLALISPT REKIAGSLIS
//