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 27-MAR-2024, entry version 99.
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; Bacillota; 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 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 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 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..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
//
