ID   SYL_LEPCP               Reviewed;         887 AA.
AC   B1XXY5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Lcho_0479;
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX   NCBI_TaxID=395495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-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; CP001013; ACB32754.1; -; Genomic_DNA.
DR   RefSeq; WP_012345516.1; NC_010524.1.
DR   AlphaFoldDB; B1XXY5; -.
DR   SMR; B1XXY5; -.
DR   STRING; 395495.Lcho_0479; -.
DR   EnsemblBacteria; ACB32754; ACB32754; Lcho_0479.
DR   KEGG; lch:Lcho_0479; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001693; 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   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; Reference proteome.
FT   CHAIN           1..887
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091333"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           644..648
FT                   /note="'KMSKS' region"
FT   BINDING         647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   887 AA;  97733 MW;  36C42A1C68EF7FDD CRC64;
     MNEKYDPAAI ESAAHAQWVA ADAYRVDENA RDSQGQLKPK FYACSMLPYP SGKLHMGHVR
     NYTINDMLTR QLRMKGMNVL MPMGWDAFGL PAENAALKNS VPPEKWTREN IATMKGQMLA
     MGLAIDWSRE VATCDPTYYK WNQWLFLKML EAGIAERRTQ VVNWDPVDQT VLANEQVIDG
     RGWRSGALVE KREIPGYYLN IVKYADELLG AVANPEDPNY LSGWPERVRL MQENWIGKSE
     GVRFAFPHQI AGADGELIQG GKLYVFTTRA DTIMGVTFCA VAPEHPLAAH AAATNPALAA
     FIAECAHGGT TEAELATQEK KGLPTGLFVT HPLTGAQVEV WVGNYVLMSY GDGAVMGVPA
     HDERDFAFAK KYGISIRQVV QAEGQTFSLD GWADWYGDKQ RAVCVNSGLL DGLPYKEAVS
     KVAELVGAQG LGEKKTTWRL RDWGISRQRY WGTPIPIIHC DDCGSVPVPE KDLPVVLPID
     CVPDGSGNPL KKRTDFLNVA CPCCGKPAQR ETDTMDTFVD SSWYFMRYCD ARNSEQMVAG
     GTDYWMPMDQ YIGGIEHAIL HLLYARFWTK VMRDLGLVKV NEPFTKLLTQ GMVLNHIYSR
     RTDKGGIEYF WPHEVENVFD AGGKVTGAKL KSDGSAVDYG GIGTMSKSKN NGVDPQDLIN
     QYGADTARLF VMFASPPEQT LEWNDAGVEG AHRFLKRVWG FGVKQAELLK GATEVGAELS
     GDAKALRREV HLVLRQVSYD YERMQYNTVV SGSMKLLNAL EAYKHDGSAG SAAVLREGYS
     VLLRGLYPAC PHITHHLWSE LGYAAKLGDL LDAPWPEVVE AALVQDEIEL VLQVNGKTRG
     SIKVPAAADK AAIEAAAAAS AEVAKFADGK PIRKLIVVPG RLVNVVV