ID SYL_RICPU Reviewed; 835 AA. AC C4K297; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 07-JUL-2009, sequence version 1. DT 24-JAN-2024, entry version 77. 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=RPR_05595; OS Rickettsia peacockii (strain Rustic). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=562019; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rustic; RX PubMed=20027221; DOI=10.1371/journal.pone.0008361; RA Felsheim R.F., Kurtti T.J., Munderloh U.G.; RT "Genome sequence of the endosymbiont Rickettsia peacockii and comparison RT with virulent Rickettsia rickettsii: identification of virulence factors."; RL PLoS ONE 4:E8361-E8361(2009). 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; CP001227; ACR47694.1; -; Genomic_DNA. DR AlphaFoldDB; C4K297; -. DR SMR; C4K297; -. DR KEGG; rpk:RPR_05595; -. DR HOGENOM; CLU_004427_0_0_5; -. DR OMA; TFMVLAP; -. DR Proteomes; UP000005015; 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; 2.20.28.290; -; 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-RELATED; 1. DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 2. 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..835 FT /note="Leucine--tRNA ligase" FT /id="PRO_1000202228" FT MOTIF 36..46 FT /note="'HIGH' region" FT MOTIF 602..606 FT /note="'KMSKS' region" FT BINDING 605 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 835 AA; 96422 MW; 57C124CBC3C0597E CRC64; MNQIEQKWQY IWQEEKAFEV SNASSKPKYY VLEMLPYPSG KIHVGHVRNY SIGDVIARFM TMQGFNVLHP MGWDAFGLPA ENAAIKNNSH PKKWTYSNIK NMKKQLKSMG FSYDWSREIN SCDPEYYKHE QKFFLELYER NLAYQKASFV NWDPVDNTVL ANEQVVDGRG WRSGAIVAKR YLKQWFLKIT DYAEELLNEI QNLKEWPEAV RSMQEKWIGK SIGANFHFKI KDNEETTIEV FSTKPETIFG ASFIGIAFNH PIIERLVSKT PEILAFITQC SHITRSSELE KAEKEGVFTG LFVTHPFDSN IVLPVIITNF VLMDYGTGAI FGCPAHDECD HELAVKMNLS IKQVIKADMD VQKTAYTEDG ILINSDVLNG LTSNEAKQEV IGEFEKLGIG KRSVNYRLKD WGISRQRFWG CPIPMIHCEI CGIVPVPYKD LPVTLPDDVN FDGHGNPLDH HPSWKHVNCP KCDKPAVRET DTFDTFFESS WYFTRYCNSN ATEMTDKKAC DYWLPVDKYI GGIEHAVMHL LYARFFTKVM NEQNYVSVRE PFKGLFTQGM VLHATYKDEH NNWLYPEEVV KKGNEFFHKE SNNRVVQGRI EKMSKSKKNL IDLETMQEQY GADAIRLFVL SDSPPEKDLE WSASGIEGCS RFINKLEYMF KAIDSLKDDV NSEVNKELNR LVHFTIKHVA EDIKHFALNR AIARMRELSN AISAEISKDK IDVKIVRHGF NVLVQLLNPF IPHITEEIWQ KLGNKERLYN LSFPAFDESM LELDTYIMAV QVNGKLRDTY EFKTSVSEDE IKQVTVSLPK VQKCLEGKEP KKIILVPRKI VNILV //