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   03-AUG-2022, entry version 72.
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=RPR_05595;
OS   Rickettsia peacockii (strain Rustic).
OC   Bacteria; Proteobacteria; 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}.
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DR   EMBL; CP001227; ACR47694.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4K297; -.
DR   SMR; C4K297; -.
DR   EnsemblBacteria; ACR47694; ACR47694; RPR_05595.
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   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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..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