ID   SYL_LEVBA               Reviewed;         809 AA.
AC   Q03RH7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=LVIS_1062;
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC   947 / NCTC 947;
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; CP000416; ABJ64195.1; -; Genomic_DNA.
DR   RefSeq; WP_011667825.1; NC_008497.1.
DR   AlphaFoldDB; Q03RH7; -.
DR   SMR; Q03RH7; -.
DR   STRING; 387344.LVIS_1062; -.
DR   EnsemblBacteria; ABJ64195; ABJ64195; LVIS_1062.
DR   KEGG; lbr:LVIS_1062; -.
DR   PATRIC; fig|387344.15.peg.1038; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001652; 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   Gene3D; 3.90.740.10; -; 1.
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..809
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009357"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           581..585
FT                   /note="'KMSKS' region"
FT   BINDING         584
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   809 AA;  92230 MW;  59458C2565B219C9 CRC64;
     MAYKHQIIER KWQHYWRANH TFETSDSQTK PKYYVMDMFP YPSGQGLHVG HPEGYTATDI
     MARLKRMQGF NVLHPMGWDA FGLPAEQYAL KTGHNPKDFT AHNIKNFKRQ IRSLGFSYDW
     SREINTTDES YYKWTQWIFE QLYKKGLAYE DKIMVNWAPD FMGGTVVANE EVIDGKTERG
     GYPVYRVPMR QWVLKITAYA DRLIDDLDDL DWPDSIKEMQ RNWIGRSEGA SVFFPVDGQA
     DTKIEVYTTR PDTLFGATYM VLAPEHAAVA KITTPEQADA VKAYQEAIES KSDLERTDLN
     KDKTGVFTGA YGINPLSGKK LPIWIGDYVL SSYGTGAIMA VPAHDERDHE FATKFNLPIT
     QVIEGDADTD ITEAAYTDDG KHINSDFMNG MDKQTAISAA IDWLTEHDAG HKQVNFRLRD
     WIFSRQRYWG EPIPVIHWEN GETTLVPEDE LPLKLPAAKQ LEPSGTGESP LANLDDWVNV
     VDENGRKGKR ETNTMPQWAG SSWYFLRYVD PTNDQAIADP EKLKYWMPVD LYIGGAEHAV
     LHLLYARFWH KFLYDLGVVP TKEPFQKLVN QGMILGTNHE KMSKSKGNVI NPDEIVEKHG
     ADTLRLYEMF MGPLEASKPW STEGINGSRR WLDRVWRLLI DDNNRLRDRV TMINDGALDK
     IYNQTVKTVT EDLEAMRFNV AISQLMVFVN EAYKVDSLPM IYMEGFVKLI SPIVPHIAEE
     LWSLLGHDET IAYAKWPTYD AKQLVEDVVE LVVQVNGKVR AHLKVAKDAT KDAIEAAALA
     DETVQVHTDG KTVRKVIVVP GKLVNIVAN