ID   SYL_RALPJ               Reviewed;         877 AA.
AC   B2UCA1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Rpic_2983;
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) 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; CP001068; ACD28106.1; -; Genomic_DNA.
DR   RefSeq; WP_012436397.1; NC_010682.1.
DR   AlphaFoldDB; B2UCA1; -.
DR   SMR; B2UCA1; -.
DR   STRING; 402626.Rpic_2983; -.
DR   EnsemblBacteria; ACD28106; ACD28106; Rpic_2983.
DR   KEGG; rpi:Rpic_2983; -.
DR   PATRIC; fig|402626.5.peg.4119; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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   Gene3D; 3.90.740.10; -; 1.
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   PANTHER; PTHR43740; PTHR43740; 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; 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..877
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091349"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           636..640
FT                   /note="'KMSKS' region"
FT   BINDING         639
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   877 AA;  97691 MW;  F3F20541DD6871B0 CRC64;
     MQDKYSPSDV EQQAQQHWQA LDAYRVTEHA RAADGSDKPK FYACSMLPYP SGKLHMGHVR
     NYTINDVMTR QLRMKGYNVL MPMGWDAFGM PAENAALNNG VAPAAWTYDN IAYMKKQMQS
     MGLAIDWSRE VATCSPDYYR WNQWLFLKML EKGIAYRKTG TVNWDPVDQT VLANEQVIDG
     RGWRSGAVVE KREIPMYYLG ITKYAQELLS DLDPLGWPER VKLMQQNWIG KSEGVRFAFP
     HNISGDDGKL INDGKLYVFT TRADTIMGVT FCAVAAEHPI ATHAAQSNPA LAAFIEECKH
     GSVMEADMAT MEKKGMPTGL TVTHPLTGES VPVWVGNYVL MTYGDGAVMG VPAHDERDFA
     FANKYHLPIK QVIDVKGQSY DTTTWADWYG DKEHGVLFHS GKYDGLNYQQ AVDAVAADLA
     AQGLGEKKTT WRLRDWGISR QRYWGTPIPL IHCESCGVVP VPEQDLPVRL PEDLVPDGTG
     NPLAKDPRFL NCTCPSCGKP ARRETDTMDT FIDSCWYYMR YTCPDGETMV DARNDYWMPM
     DQYIGGIEHA ILHLLYARFW TKVMRDLGLV KFDEPFTNLL TQGMVLNETY YREDASGKKQ
     WINPADVDVQ TDERGRPVGA TLKADGQPVV IGGVEKMSKS KNNGIDPQAL IDQYGADTAR
     LFTMFAAPPE QQLEWNDAGV EGASRFLRRL WNFGVVHGDA IRGGHGNGVV AGATDADRAL
     RRELYTVLKQ ANYDYERLQY NTVVSATMKM LNALEGAKDA GADARREGLG LLLRVLYPVV
     PHITHVLWTE LGYAGAYGDL LDAPWPQVDE GALVQSEIEL VLQVNGKVRG SIVVPADADR
     AAIEAIAAKD EAVQKFAEGK PPKKIIVVPG RLVNVVA