ID   SYL_RICRS               Reviewed;         835 AA.
AC   A8GS16;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=A1G_03300;
OS   Rickettsia rickettsii (strain Sheila Smith).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=392021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheila Smith;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia rickettsii.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000848; ABV76191.1; -; Genomic_DNA.
DR   RefSeq; WP_012150778.1; NZ_CP121767.1.
DR   AlphaFoldDB; A8GS16; -.
DR   SMR; A8GS16; -.
DR   GeneID; 79937331; -.
DR   KEGG; rri:A1G_03300; -.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000006832; 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; 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_1000009418"
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
//