ID   SYL_LACCB               Reviewed;         803 AA.
AC   B3WCD5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=LCABL_09490;
OS   Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=543734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL23;
RA   Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA   Deutscher J.;
RT   "Lactobacillus casei BL23 complete genome sequence.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; FM177140; CAQ66036.1; -; Genomic_DNA.
DR   RefSeq; WP_003578174.1; NC_010999.1.
DR   AlphaFoldDB; B3WCD5; -.
DR   SMR; B3WCD5; -.
DR   KEGG; lcb:LCABL_09490; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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; 2.
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.
FT   CHAIN           1..803
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091325"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           575..579
FT                   /note="'KMSKS' region"
FT   BINDING         578
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   803 AA;  91527 MW;  487E45B7E7F7BA4B CRC64;
     MAYDHHEIDK KWQRYWAEHN EFNTTTDPKK PNYYALDMFP YPSGQGLHVG HPEGYTATDI
     VARMKRMQGF NVLHPMGWDA FGLPAEQYAL NTGHNPKTFT KQNIETFKRQ INSLGFSYDW
     NREINTTDPN YYKWTQWIFE QLYKHGLAYE AEVPVNWSPD LGTVVANEEV IDGKTERGGF
     PVVRKPMRQW MLKITAYAEK LLTDLDDLDW PESIKQMQRN WIGKSTGAQI TFRVTDSHEP
     FDVFTTRPDT LFGATYVVMA PEHELVQKIT TPAQQAVVDA YIDEAAHKSD LDRTALDKEK
     TGVWTGAYAT NPVNGEKLPI WISDYVLASY GTGAIMSVPA HDDRDYAFAK KFGIEIKPVI
     EGGNVDEAAY TGDGVHINSG FLDGLNEHDA IDRMIKWLED KGIGSAKINY KLRDWVFSRQ
     RYWGEPIPVI HWEDGETTLV PEDELPLTLP EEADIKPSGT GESPLANLTD WVNVVDKNGR
     KGKRETNTMP QWAGSSWYFL RFVDPHNKEA LADYDKLKAW MPVDLYIGGA EHAVLHLLYA
     RFWNLFLYDI GAIPNKEPFQ RLFNQGMILG DNHEKMSKSK GNVVNPDDVV DEYGADTLRL
     YEMFMGPLDA GIAWSTKGLA GARKFLDRVW SAFIDDEGKL RDRITTINDG RLDKVYNETV
     KKVTEDYDAL HFNTAISQMM VFINSARKDD DLPLEYVEGF VKMLAPIAPH LMEEIWSRLG
     HDHSLTYAPW PSYDESKIKT DTYDMMIQVN GKLRGSITAD VNESDDEIKQ AALANDNVQK
     FTAGKDIKKI IVVPRKIVNI VAK