ID   SYL_RICCK               Reviewed;         834 AA.
AC   A8EZ02;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=A1E_03250;
OS   Rickettsia canadensis (strain McKiel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=293613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=McKiel;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia canadensis.";
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; CP000409; ABV73585.1; -; Genomic_DNA.
DR   RefSeq; WP_012148781.1; NC_009879.1.
DR   AlphaFoldDB; A8EZ02; -.
DR   SMR; A8EZ02; -.
DR   STRING; 293613.A1E_03250; -.
DR   PRIDE; A8EZ02; -.
DR   EnsemblBacteria; ABV73585; ABV73585; A1E_03250.
DR   KEGG; rcm:A1E_03250; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000007056; 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..834
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009417"
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   834 AA;  96715 MW;  F03D4890B99F6947 CRC64;
     MNQIEQKWQQ IWDDEKAFEV SNECNKPKYY VLEMLPYPSG KIHVGHVRNY SIGDVIARFM
     NMQGFNVLHP MGWDAFGLPA ENAAIKNNVH PKEWTYSNVD NMQQQLKSMG FAYDWSRVIN
     SCDPQYYKYE QKFFLELYER NLAYQKEALV NWDPVDNTVL ANEQVVDGRG WRSGAIIEKR
     YLKQWFLKIT DYAEELLNEI KNLKEWPEAV RSMQEKWIGK SIGANFYFKV KDNEDAIIEV
     FSTKPETIFG ASFIGIAFNH PIIEKLISKT PEISNFITKC LHITGSSELE KAEKDGILTS
     LYVIHPFDPS IILPVIITNF VLMDYGTGAI FGCPAHDERD HELAVKMNLP IKQVIEADID
     VHKIAYTEDG ILINSDFLNG LTNNEAKQKV IKEIEKLQIG KRSINYRLKD WGISRQRFWG
     CPIPMIYCKV CDIVPVPYKD LPVTLPDNVK FNGHGNPLDH HPTWKHVNCP KCDKPAIRET
     DTFDTFFESS WYFTRYCNSH ATDMTDKKAC DYWLPVDKYI GGIEHAVMHL LYARFFTKVM
     NEQNYVSVRE PFKGLFTQGM VLHATYKDEH NNWLYPDEVV KKDNKFFHKK SGNLVVQGRI
     EKMSKSKKNL IDLETMQKQY GADAIRLFVL SDSPPEKDLE WSVSGLEGCS RFINKLEHMF
     KVIASLKDDV TGINKELNRL VHLTIKYVAE DIKHFALNRA IARMRELSNA ISSEFSKEVM
     DVKTVKYGFN VLVQLLNPFI PHITEEIWQK LGNKERLYKT AFPAFDESML ELDTYVMAVQ
     VNGKLRDTYE FNNSASDYEI KQITINLPKV QKFLEGTEPK KIIFVPRKIV NIIV