ID   SYL_LACDB               Reviewed;         804 AA.
AC   Q049B7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
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};
GN   OrderedLocusNames=LBUL_1451;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-365 / Lb-18;
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}.
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DR   EMBL; CP000412; ABJ58955.1; -; Genomic_DNA.
DR   RefSeq; WP_011678469.1; NC_008529.1.
DR   AlphaFoldDB; Q049B7; -.
DR   SMR; Q049B7; -.
DR   KEGG; lbu:LBUL_1451; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   BioCyc; LDEL321956:LBUL_RS06850-MONOMER; -.
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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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.
FT   CHAIN           1..804
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334767"
FT   MOTIF           39..50
FT                   /note="'HIGH' region"
FT   MOTIF           573..577
FT                   /note="'KMSKS' region"
FT   BINDING         576
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   804 AA;  91939 MW;  BA9ACA2304EC60F0 CRC64;
     MYNHKVVEKK WQKYWLENKT FKTGTDPEKP KYYVLDMFPY PSGKGLHVGH PEGYTATDIM
     ARMKRAQGYN VLHPMGWDAF GLPAEQYALQ TGNDPATFTD ENIAHFKKQL QALGFSYDWD
     REIKTTDPNY YKWTQWIFEQ MYKMGLAYEA EVPVNWSPDL GTVVANEEVI DGKTERGGYP
     VYRRKMRQWM LKITAYADRL LDDLDDLDWP EPIKEMQRNW IGRSVGAQVT FKIKDSDKSF
     AVFTTRPDTL FGCSYTVLAP ENELVKEITS PEQKEAVDAY IKSIESKSDL ERTDLNKDKT
     GVFTGAYAIN PVNGEEVPVW ISDYVLATYG TGAVIAVPAH DERDYAFATK FDLPIKEVVE
     GGDISKEAFA GDGVHVNSDF LNGLHNEEAK AKMVDWLTEK GVGEKKVNYK MRDWNFSRQR
     YWGEPIPVIH WEDGETTLVP EDELPLRLPK ESNIKPSGTP ESPLANLTDW VNVVDENGRK
     GKRETNTMPQ WAGSSWYFLR YIDPHNDKAL ADPELLKKWM PVDLYIGGAE HATLHLLYAR
     FWHKVLYDLG VVPTKEPFQK LYNQGLILKN HEKMSKSRGN VVNPDDVVDE YGADSLRTYE
     MFMGPLNASI DWDDNGPSGV KKFLDRVWRT FVNDLDLDPI PSEKITDKND GKLDKIYNET
     VKTVTEHFEE LRFNTAISQM MVFMNACQKV DKIPREYAEG FVKLMAPVAP HMMEEIWHVF
     GHDESVQFAA WPTYDASKLV ESTVEMAVTV NGKKRGNFQI AKDASREEAQ AAATALPHVK
     EFLEGKEIKK VIVVPNKIVN IVAK
//