ID   SYL_BACC0               Reviewed;         802 AA.
AC   B7JT07;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
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=BCAH820_4861;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-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; CP001283; ACK89591.1; -; Genomic_DNA.
DR   RefSeq; WP_000009448.1; NC_011773.1.
DR   AlphaFoldDB; B7JT07; -.
DR   SMR; B7JT07; -.
DR   GeneID; 45024607; -.
DR   KEGG; bcu:BCAH820_4861; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   Proteomes; UP000001363; 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   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..802
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199177"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   802 AA;  91273 MW;  0C8DF07756FD0FFD CRC64;
     MSFNHQEIEK KWQGYWEENK TFRTPDETEK PKFYALDMFP YPSGAGLHVG HPEGYTATDI
     LSRMKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNSPAEFT EHNINTFRNQ IKSLGFSYDW
     DREVNTTDPN YYKWTQWIFL KLFEKGLAYV DEVPVNWCPA LGTVLANEEI IDGKSERGGH
     PVERRPMRQW MLKITAYGDR LLEDLDELDW PESLKDMQRN WIGRSEGAEV HFNIDGTDEK
     FTVFTTRPDT LFGASYCVLA PEHALVADIT TADQKEAVEA YINSVKMKSD LERTELAKEK
     TGVFTGAYAV NPVNGEKLPI WIADYVLATY GTGAVMAVPA HDERDYEFAS TFNLPMKEVV
     KGGDITKEAY TGDGAHVNSA FLDGLNKEEA IAKMIEWLEV TSAGNQKVTY RLRDWLFSRQ
     RYWGEPIPVI HWEDGTMTAV KEEELPLVLP KTENIRPSGT GESPLANIDE WVNVVDPETG
     KKGRRETNTM PQWAGSCWYY LRYIDPNNSE ALVDPEKVKQ WLPVDIYIGG AEHAVLHLLY
     ARFWHKVLYD IGVVPTKEPF QQLFNQGMIL GENNEKMSKS KGNVVNPDDI VASHGADTLR
     LYEMFMGPLD ASIAWSENGL DGARRFLDRV WRLFVQDNGE LSEKITDAPN KDLEKAYHQT
     VKKVTEDYAE LRFNTAISQM MVFINDAYKA ETLPKEYVEG FVKMIAPVAP HIGEELWSKL
     GYNETITYAS WPTFDESKLV EDEVEIVVQV MGKVRAKLTM SKDASKDEME KLALEAIQDQ
     IEGKTVRKVI VVPGKLVNVV AN
//