ID   SYM_CUTAK               Reviewed;         601 AA.
AC   Q6A707;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 122.
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}; OrderedLocusNames=PPA1728;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(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_00098}.
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_00098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00098};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00098};
CC   -!- SUBUNIT: Monomer. {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; AE017283; AAT83457.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6A707; -.
DR   SMR; Q6A707; -.
DR   STRING; 267747.PPA1728; -.
DR   EnsemblBacteria; AAT83457; AAT83457; PPA1728.
DR   KEGG; pac:PPA1728; -.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_1_2_11; -.
DR   OMA; YMRMAGH; -.
DR   Proteomes; UP000000603; 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:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.20.28.20; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR   InterPro; IPR041872; Anticodon_Met.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR45765; PTHR45765; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF57770; SSF57770; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN           1..601
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139153"
FT   MOTIF           21..31
FT                   /note="'HIGH' region"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
SQ   SEQUENCE   601 AA;  66602 MW;  78F59DD053CE9390 CRC64;
     MSATDRVNLM CANVLAAVAW PYANGPRHIG HVSGFGVPSD VFARYMRMSG HRVLMVSGSD
     CHGTAISVKA DQEGVTAQEC AEKYHRIIAA DLQGLGLSYD LYTSTLTDNH AHVTQEIFTR
     LHENGYVVKR SEMGAFEPST GRTLPDRYIE GTCPVCGYDD ARGDQCDNCG RQLDPADLIG
     PRSKTTGAAP EFRETEHFFL DLPALAESLA SWIDTRTDWR PNVLKFSHNL LEELRPRAIT
     RDLDWGIRVP VEGWQDNPMK SIYVWFDAVI GYLSASIEWA RRIGRPDAWR EFWNDEDARS
     YYFMGKDNIV FHSVIWPGIL LGTNGRGDKG GEPSEELGTL NLPTEIVSSE FLTMSGSKVS
     NSRGATIFVG DFLHEFGPDA LRYFIAVAGP ENQDTDFTWE EFVRRVNFEL ANEWGNLVNR
     SISMAFKNCH EIPAAGELTD ADRELLDAAA AGFDTVGGLL AHARFKAAIT EAMRIVGLAN
     AYISAEEPWK LKDNPERRDT VLHVALQVVS DVNTMMTPFM PHSAQKIYEA LGGEGVWAAQ
     PELIETDGAP ILMGDYATEQ ASWGRHEITV GTPLSKPSPI FRKLDAKLAQ TGPQWAPVNP
     Q