ID   SYM_BORAP               Reviewed;         724 AA.
AC   Q0SMS1; G0IQD7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 117.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00098};
DE            EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_00098};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00098};
DE            Short=MetRS {ECO:0000255|HAMAP-Rule:MF_00098};
GN   Name=metG {ECO:0000255|HAMAP-Rule:MF_00098};
GN   OrderedLocusNames=BAPKO_0618, BafPKo_0603;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC   Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
CC   -!- FUNCTION: Catalyzes the attachment of L-methionine to tRNA(Met). Is
CC       required not only for elongation of protein synthesis but also for the
CC       initiation of all mRNA translation through initiator tRNA(fMet)
CC       aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Met) + L-methionine + ATP = L-methionyl-tRNA(Met) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-
CC         COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215;
CC         EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13482;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00098};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00098};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00098}.
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DR   EMBL; CP000395; ABH01857.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69807.1; -; Genomic_DNA.
DR   RefSeq; WP_004789630.1; NC_008277.1.
DR   AlphaFoldDB; Q0SMS1; -.
DR   SMR; Q0SMS1; -.
DR   STRING; 29518.BLA32_01330; -.
DR   GeneID; 77265433; -.
DR   KEGG; baf:BAPKO_0618; -.
DR   KEGG; bafz:BafPKo_0603; -.
DR   PATRIC; fig|390236.22.peg.580; -.
DR   eggNOG; COG0073; Bacteria.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_3_2_12; -.
DR   OrthoDB; 9810191at2; -.
DR   Proteomes; UP000005216; Chromosome.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:TreeGrafter.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:InterPro.
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; cd02153; tRNA_bindingDomain; 1.
DR   FunFam; 2.20.28.20:FF:000001; Methionine--tRNA ligase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR   Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR004495; Met-tRNA-synth_bsu_C.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR029038; MetRS_Zn.
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   NCBIfam; NF001100; PRK00133.1; 1.
DR   PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 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; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding; Zinc.
FT   CHAIN           1..724
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000331786"
FT   DOMAIN          560..665
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   MOTIF           330..334
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         333
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
SQ   SEQUENCE   724 AA;  84391 MW;  3D8839B7529646D9 CRC64;
     MKKMNLITAA LPYVNNIPHL GNLVQVLSAD AFARYSKMSG IETLYICGTD EYGTATETKA
     LIEKTTPLEL CNKYYEIHKS IYKWFNIEFD IFGRTTNKHH QETVQNFFLK LEKNGYIKER
     ETEQFFCNKD LIFLADRYVI GECPECQSMA KGDQCDNCSK LLNPTDLINP KCIICKNKPI
     LKKTNHLYID LPKIKTKLEK WIKNPTTSKN WNTNALKMTN AFLRDGLKER AITRDLKWGI
     PVPKKGYENK VFYVWFDAPI GYISITKNIV KNWESWWKNN KQVNLVQFIG KDNILFHTIM
     FPCIKIGSKE NWTTLNQLSS SEYLNYENLK FSKSEGTGIF GNDVITTGIP SDVWRFYIYY
     NRPEKSDFQF IWQDLMERVN TELIDNFSNL VNRVLTFQKK FFGDVIETIE IQHKFWEQIT
     PKYNKILNLF KNTELKSALK EILKISSFGN KIFQDNEPWK RKESSPQEIK ELILNLIYLI
     RDLSILMMPF IPETSKKIQQ FFGNSYQFST KILGTKSGIK KIEFVEILFN KLEQKKINDL
     RLKYSGEKNM KEKEQPENLF REKVLLRVVK INKIERNPEA KNLFILKLDD GTNKDKQIVS
     SLEGYYTEEE LLGKHIIIVD NLKPAKFRGI KSEGMLIAAE DKNKNFKIII VEDSIKNPIA
     GERIILENDQ NKDLTCPPKI DINKFSKANI ITENGELKIN GINLILEHSK NKILSKDIPN
     GIVC
//