ID   SYL_RICFE               Reviewed;         835 AA.
AC   Q4ULS1;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=RF_0651;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(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}.
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DR   EMBL; CP000053; AAY61502.1; -; Genomic_DNA.
DR   RefSeq; WP_011270981.1; NC_007109.1.
DR   AlphaFoldDB; Q4ULS1; -.
DR   SMR; Q4ULS1; -.
DR   STRING; 315456.RF_0651; -.
DR   EnsemblBacteria; AAY61502; AAY61502; RF_0651.
DR   KEGG; rfe:RF_0651; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008548; 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_0000277916"
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;  96428 MW;  3231450DC4964218 CRC64;
     MNQIEQKWQQ IWYDEKAFEV SNESSKPKYY VLEMLPYPSG KIHVGHVRNY SIGDVIARFM
     TMQGFNVLHP MGWDAFGLPA ENAAIKNNSH PKDWTYSNIE NMKKQLKSMG FSYDWSREIN
     SCDPQYYKHE QKFFLELYER NLAYQKESLV NWDPVDNTVL ANEQVVDGRG WRSGAIVEKR
     YLKQWFLKIT DYAEELLNEI QNLKEWPEAV RSMQEKWIGK SIGANFHFKI KDNEDNTIEV
     FSTKPETIFG AGFIGIAFNH PIIEKLISKT PEILSFITKC SHITGSSELE KTEKEGVFTG
     LYVIHPFDSN IVLPVIITNF VLMDYGTGAV FGCPAHDERD HELAVKMNLP IKQVIETDID
     VQKTAYTEDG ILVNSDFLNG LTSNEAKQKV IDEFEKLGIG KRSVYYRLKD WGISRQRFWG
     CPIPMIHCEA CGIVPVPCSD LPVTLPDDVS FDGHGNPLDH HPSWKHVNCP KCDKSAIRET
     DTFDTFFESS WYFTRYCNSN ATEMTDKKAC DYWLPVDKYI GGIEHAVMHL LYARFFTKVM
     NEQNYVSVRE PFKGLFTQGM VLHATYKDEH NNWLYPEEVV KKGNEFFHKE SNNRVVQGRI
     EKMSKSKKNL IDLVTMQEQY GADAIRLFVL SDSPPEKDLE WSASGIEGCS RFINKLEHMF
     EAIASLIDDV NSEINKELNR LVHFTIKHVA DDIKHFVLNR AIARMRELSN AISAELNKEV
     VDVKTVRYGF NVIVQLLNPF IPHITEEIWQ KLGNKERLYN SAFPAFDESM LELDTYVMAV
     QVNGKLRDTY EFKTSASEDE IKQITVNLPK VQKFLEGKEP KKIILVPRKI VNIIV