ID SYL_LATSS Reviewed; 807 AA. AC Q38VP5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 120. 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=LCA_1436; OS Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei OS subsp. sakei). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Latilactobacillus. OX NCBI_TaxID=314315; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=23K; RX PubMed=16273110; DOI=10.1038/nbt1160; RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M., RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V., RA Zagorec M.; RT "The complete genome sequence of the meat-borne lactic acid bacterium RT Lactobacillus sakei 23K."; RL Nat. Biotechnol. 23:1527-1533(2005). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR936503; CAI55738.1; -; Genomic_DNA. DR RefSeq; WP_011375128.1; NC_007576.1. DR AlphaFoldDB; Q38VP5; -. DR SMR; Q38VP5; -. DR STRING; 314315.LCA_1436; -. DR KEGG; lsa:LCA_1436; -. DR eggNOG; COG0495; Bacteria. DR HOGENOM; CLU_004427_0_0_9; -. DR OrthoDB; 9810365at2; -. DR Proteomes; UP000002707; 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; Reference proteome. FT CHAIN 1..807 FT /note="Leucine--tRNA ligase" FT /id="PRO_1000009362" 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 807 AA; 92127 MW; 38344640F2DCE7B3 CRC64; MTYDHRAVEQ KWQAYWQSHK SFKTTEDKDK KNFYALDMFP YPSGQGLHVG HPEGYTATDI LARMKRMQGF NVLHPMGWDA FGLPAEQYAL DTGNNPADFT QKNINTFKRQ INSLGFSYDW DREVNTTDPD FYKWTQWIFE KMYEKGLAYE AEVAVNWSPD LGTVVANEEV IDGKTERGGY PVYRKPMRQW MLKITAYADR LIDDLDLVDW PESVKDMQRN WIGRSKGAEV SFAVENHDAN IDVFTTRADT MFGVSYIVMA PEHKLVADIT TPEQKAAVDA YLKEIEHKSD LERTDLAKDK TGAFTGAYAI NPVNGERLPI WISDYVLASY GTGAVMAVPA HDPRDWEFAK KFGLPLKPVV SGGNPEEAVH TEPGVMINSD FLDGLDKQAA IDKMIPWLVE HKVGHEQISY KLRDWLFSRQ RYWGEPIPII HWEDGTTSVV PEDQLPLELP LTSDIKPSGT GESPLANLTD WLNVTDENGR KGRRETNTMP QWAGSSWYYL RYIDPKNPDK LADFDKLKDW LPVDMYIGGA EHAVLHLLYV RFWHKFLYDI GVVPTKEPFQ HLYNQGMILG DNHEKMSKSK GNVVNPDDVV DRFGADTLRL YEMFMGPLDA SISWSEKGLA GARKFLDRVW RLYTEEDTDE NDQLSSKIVA DNNDQLKKVY NETVKKVTED FESMHFNVAI SQLMVFINDA YKADTFPREY AEGFVKLLAP IAPHMMEELW AMLGHDDSIS YVDWPTFDPA ALIANEVEVI FQVNGKLKAK VTVAKDTPKE ELEAMAKANE KVAEFIADKT VRKVIAIPNK LVNIVAN //