ID   SYL_OENOB               Reviewed;         810 AA.
AC   Q04FL2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=OEOE_0839;
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=203123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ56760.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000411; ABJ56760.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002818743.1; NC_008528.1.
DR   AlphaFoldDB; Q04FL2; -.
DR   SMR; Q04FL2; -.
DR   STRING; 203123.OEOE_0839; -.
DR   PRIDE; Q04FL2; -.
DR   EnsemblBacteria; ABJ56760; ABJ56760; OEOE_0839.
DR   KEGG; ooe:OEOE_0839; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000774; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..810
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334785"
FT   MOTIF           41..52
FT                   /note="'HIGH' region"
FT   MOTIF           582..586
FT                   /note="'KMSKS' region"
FT   BINDING         585
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   810 AA;  93102 MW;  69B5134C35CB569A CRC64;
     MSYDHKAIEK RWQTYWDEHK TFKTAPETSG KPKYYVMNMF PYPSGQGLHV GHPESYTATD
     IMARFNRMRG FNVLQPMGWD AFGLPAEQYA IKTGHNPADF TNENIKHFKK QVKSLGFSYD
     WDREINTTDP EYYKWTQWIF EQLYKKGLAY EDEIMVNWAP DFPGGGIVVA NEEVIDGKTE
     RGSYPVYRVP MKQWVLRITK YAERLLSDLD DLDWPEAIKE QQRNWIGKST GAAVFFKVDG
     KSDYQVEVYT TRPDTLFGAS YMVLAPEHDL VDKITTSECR ADVDAYKAKI ASKSDLERTD
     LNREKTGAFT GAYGINPVNG EKIPIWIADY VLSSYGTGAI MAVPAHDTRD YEFAKKFDLP
     IRQVIKGGDI SKEAFTGDGT HINSAFLDVL DKKQAIEKII DWLEEHDAGH KQVNYKLRDW
     IFSRQRYWGE PIPVIHWEDG KQTLVPESEL PLRLPHLNQD QMKPSGTGES PLANAKSWLE
     VTRQDGVKGR RETNTMPQWA GSSWYFLRYI DPHNDKVLAD PEKLKYWMNV DLYVGGAEHA
     VLHLLYARFW HKFLYDLGIV PTKEPFQKLV NQGMILGTNH EKMSKSKGNV VNPDEIVDSY
     GADALRVYEM FMGPLTQSKP WSTESLAGIR RYLDRVWRIF TSDGDGINPI IVSENDHKLD
     KIFNQTVKKV TEDYAAMRFN TAISQMMVFI NETFKAEKLP KKYMNAFLQL LNPVAPHITE
     ELWQRMGHQE TIAYATWPTY DESQIIEKQI EMAVQINGKV RAKINTPVDI SRDELAKMAT
     DNPDVKKQVA DKNIVKIIAI PGKIINIVVK