ID   SYL_LYSSC               Reviewed;         805 AA.
AC   B1HXY7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Bsph_4241;
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41;
RX   PubMed=18296527; DOI=10.1128/jb.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA41702.1; -; Genomic_DNA.
DR   RefSeq; WP_012295731.1; NC_010382.1.
DR   AlphaFoldDB; B1HXY7; -.
DR   SMR; B1HXY7; -.
DR   EnsemblBacteria; ACA41702; ACA41702; Bsph_4241.
DR   KEGG; lsp:Bsph_4241; -.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000002164; 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.
FT   CHAIN           1..805
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091335"
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   805 AA;  91395 MW;  BAF32FB558789C0D CRC64;
     MSFNHQQIEK KWQQYWADNK TFKTENETEK PKFFALDMFP YPSGAGLHVG HPEGYTATDI
     LSRFKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNDPAEFT AKNIATFKRQ IQELGFSYDW
     DREINTTDPA YYKWTQWIFI QLYKKGLAYV DEVAVNWCPA LGTVLANEEV IDGKSERGGH
     PVERRPMKQW MLKITAYADR LIDDLEEVDW PESIKDMQRN WIGRSEGAEV TFGIDGTDEN
     FTVFTTRPDT LFGATYCVLA PEHKLVEQIT TVEQRQAVED YLEKVKMKSD LERTDLAKEK
     TGVFTGAYAV NPINGKKVPI WIADYVLVSY GTGAIMAVPA HDERDYEFAS AFSLDIVPVL
     EGGDISKEAF TGDGQHINSD FLNGLNKVEG IAKAIEWLEE KGVGEKKISY RLRDWLFSRQ
     RYWGEPIPMI HWEDGTITPV PEEELPLMLP KTDNIRPSGT GESPLANIAE WVNVVDPATG
     KKGRRETNTM PQWAGSSWYF LRYIDPTNTE AIADPELLKR WLPVDIYIGG AEHAVLHLLY
     ARFWHKVLYD LGVVHTKEPF QKLFNQGMIL GEGNEKMSKS KGNVVNPDEI IESHGSDTLR
     LYEMFMGPLE ASVAWSTNGL DGARRFLDRI WRLLVNEEDG TISAKIQVSD DKTLEKSYHQ
     TVKKVTEDYE GIRFNTAISQ MMVFINDCYK AEVIPTAYAE GFVKMLAPIA PHIAEELWNL
     LGHEGTLSYE QWPTYDESKL VDDEVEVAVQ VAGKVRAKIV VAKDASKEDI EKVALADEKV
     QEYMAGKDLV KVIVIPGKLV NIVVK