ID   SYL_RICRO               Reviewed;         835 AA.
AC   B0BXI2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=RrIowa_0700;
OS   Rickettsia rickettsii (strain Iowa).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=452659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa;
RX   PubMed=18025092; DOI=10.1128/iai.00952-07;
RA   Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K., Porcella S.F.,
RA   Hackstadt T.;
RT   "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT   avirulent Rickettsia rickettsii Iowa.";
RL   Infect. Immun. 76:542-550(2008).
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; CP000766; ABY72558.1; -; Genomic_DNA.
DR   RefSeq; WP_012150778.1; NC_010263.3.
DR   AlphaFoldDB; B0BXI2; -.
DR   SMR; B0BXI2; -.
DR   STRING; 452659.RrIowa_0700; -.
DR   EnsemblBacteria; ABY72558; ABY72558; RrIowa_0700.
DR   GeneID; 45539156; -.
DR   KEGG; rrj:RrIowa_0700; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000796; 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_1000074841"
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;  96663 MW;  6EDD0250CFCAC379 CRC64;
     MNQIEQKWQY IWQEEKAFEV SNASSKPKYY VLEMLPYPSG KIHVGHVRNY SIGDVIARFM
     TMQGFNVLHP MGWDAFGLPA ENAAINNNSH PKKWTYSNIK NMKKQLKSMG FSYDWSREIN
     SCDPEYYKHE QKFFLELYER NLAYQKESFV NWDPVDNTVL ANEQVVDGRG WRSGAIVAKR
     YLKQWFLKIT DYAEELLNEI QNLKEWPEAV RSMQEKWIGK SIGANFHFKI KDNEETTIEV
     FSTKPETIFG ASFIGIAFNH PIIERLVSKT PEILAFITQC SHITRSSKLE KAEKEGVFTG
     LFVTHPFDSN IVLPVIITNF VLMDYGTGAI FGCPAHDECD HELAVKMNLS IKQVIKADMD
     VQKTAYTEDG ILINSDFLNG LTSNEAKQEV IREFEKLGIG KRSVNYRLKD WGISRQRFWG
     CPIPMIHCEI CGIVPVPYKD LPVTLPDDVN FDGHGNPLDH HPSWKHVNCP KCDKPAVRET
     DTFDTFFESS WYFMRYCNSN ATEMTDKKAC DYWLPVDKYI GGIEHAVMHL LYARFFTKVM
     NEQNYVSVQE PFKGLFTQGM VLHATYKDEH NNWLYPEEVV KKGNEFFHKE SNNRVVQGRI
     EKMSKSKKNL IDLETMQEQY GADAIRLFVL SDSPPEKDLE WSASGIEGCS RFINKLEYMF
     KAIDSLKDDV NSEVNKELNR LVHFTIKHVA EDIKHFALNR AIARMRELSN SISAEISKDK
     IDVKTVRHGF NVLVQLLNPF IPHITEEIWQ KLGNKERLYN LSFPAFDESM LELDTYIMAV
     QVNGKLRDTY EFKTSVSEDE IKQVTVSLPK VQKFLEGKEP KKIILVPRKI VNILV