ID   SYL_BACC4               Reviewed;         802 AA.
AC   B7H798;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=BCB4264_A4851;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
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 B4264.";
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; CP001176; ACK59437.1; -; Genomic_DNA.
DR   RefSeq; WP_000009462.1; NC_011725.1.
DR   AlphaFoldDB; B7H798; -.
DR   SMR; B7H798; -.
DR   EnsemblBacteria; ACK59437; ACK59437; BCB4264_A4851.
DR   KEGG; bcb:BCB4264_A4851; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000007096; 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.
FT   CHAIN           1..802
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199178"
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;  91339 MW;  59934062BBDF2DC8 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 LFGATYCVLA PEHALVAEIT TAEQKEAVEA YINAVKMKSD LERTELAKEK
     TGVFTGAYAV NPVNGEKLPI WIADYVLATY GTGAVMAVPA HDERDYEFAS VFNLPMKEVV
     KGGDITKEVY TGDGAHVNSA FLDGLNKEEA IAKMIEWLEA 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 KELEKAYHQT
     VKKVTEDYAE LRFNTAISQM MVFINDAYKA ETLPREYVEG FVKMIAPVAP HIGEELWSKL
     GYNETITYAS WPTFDESKLV EDEVEIVVQV MGKVRAKLTM SKDASKEEME QLALEAIQDQ
     IEGKTVRKVV VVPGKLVNVV AN