ID   SYL_RICBR               Reviewed;         831 AA.
AC   Q1RJS2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=RBE_0311;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04392.1; -; Genomic_DNA.
DR   RefSeq; WP_011477003.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJS2; -.
DR   SMR; Q1RJS2; -.
DR   STRING; 336407.RBE_0311; -.
DR   PRIDE; Q1RJS2; -.
DR   EnsemblBacteria; ABE04392; ABE04392; RBE_0311.
DR   KEGG; rbe:RBE_0311; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001951; 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..831
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000277915"
FT   MOTIF           35..45
FT                   /note="'HIGH' region"
FT   MOTIF           600..604
FT                   /note="'KMSKS' region"
FT   BINDING         603
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   831 AA;  95795 MW;  017EDD2BC037ACA9 CRC64;
     MNIEQKWQQI WQEEKAFEVP NESSKPKYYV LEMLPYPSGK IHVGHVRNYS IGDVVARFMT
     MQGFNVLHPM GWDSFGLPAE NAAIKNNSHP KEWTYSNIEN MKKQLKSMGF SYDWSREINS
     CDPDYYKHEQ KFFLELYERN LAYQKESLVN WDPVDNTVLA NEQVVDGRGW RSGAIVEKRY
     LKQWFLKITN YAEELLNEIP NLTEWPEAVR SMQEKWIGKS VGANFRFKIK DNEDVIEVFS
     TKPETIFGAS FVGIAFNHPI IEKLVSKTPE IENFIAKCSN ITGSAEFDKA EKEGIFTGLY
     VVHPFDSNIT LPVVITNFVL MDYGTGAVFG CPAHDQRDHE LAVKINLPIK QVIEADTDVQ
     KAAYTEDGII INSGFLNGLS TNEAKQRVIE EFEKLGIGKR TINYRLKDWG ISRQRFWGCP
     IPIIHCDSCG LVPVPDSDLP VTLPDDVKFD GHGNPLDNHP TWKHVNCPKC SKPAIRETDT
     FDTFFESSWY FTRYCNSQAL EMTDKKACDY WLPVDKYIGG IEHAVMHLLY ARFFTKVMNE
     QDYVSVREPF KGLFTQGMVL HATYKDEHNN WLYPEEVIKK GNEFFHKENG GLVTQGRIEK
     MSKSKKNLID LETMQQQYGA DAIRFFVLSD SPPEKDLEWS ASGIEGSARF INKLEQMQET
     IIKLSDNKNT NKELKRLIHF TIKHVAEDIK HFALNRAIAR MRELFNAISS EINKEEIDVQ
     NAKHGFNVLI QLLNPFIPHI TEEIWQKLGH KTFLYNAAFP TFDESMLELD TYVIAVQVNG
     KLRDTYEFNT SASEDEIKQI AINLPKVQKF LEGKEPKKII LVPKKIINII C