ID   SYL_LEPIN               Reviewed;         863 AA.
AC   Q8EZY7;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   27-MAR-2024, entry version 121.
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=LA_3714;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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; AE010300; AAN50912.2; -; Genomic_DNA.
DR   RefSeq; NP_713894.2; NC_004342.2.
DR   RefSeq; WP_001199945.1; NC_004342.2.
DR   AlphaFoldDB; Q8EZY7; -.
DR   SMR; Q8EZY7; -.
DR   STRING; 189518.LA_3714; -.
DR   PaxDb; 189518-LA_3714; -.
DR   EnsemblBacteria; AAN50912; AAN50912; LA_3714.
DR   KEGG; lil:LA_3714; -.
DR   PATRIC; fig|189518.3.peg.3690; -.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   InParanoid; Q8EZY7; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 3.
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   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   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; Reference proteome.
FT   CHAIN           1..863
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152036"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           635..639
FT                   /note="'KMSKS' region"
FT   BINDING         638
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   863 AA;  99581 MW;  F108F39E0356E644 CRC64;
     MQYPFQEVES FWQKFWEEHK SFQTNIRSSK PKFYCLDMFP YPSGAGLHVG HPEGYTATDI
     LSRFKRMKGF EVLHPMGWDA FGLPAERYAM QTGIHPAITT KDNIDNFRRQ IQMIGLSYDW
     SRELSTTDPD YYKFTQWIFI QLYQSWFNPE LKKAESINEL IRRFSNQGSN GLDYRQFNSE
     EWKNFSPVEK EKILSDFRLV YQAEIPVNWC EALGTVLANE EVEEWVGKGY EVVRKPMRQY
     MMRITAYADR LLEDLELVEW PPSTLEMQKN WIGKSEGLEI TFPFLKPLQS GLEGIRIFTT
     RPDTIFGVTY MVVAPEHPIV SEITTPEQKQ KVEEYQKTSS LKSDLDRMEL NKEKTGVFTG
     TFVFNPADPS QKIPVWISDY VLYGYGTGAI MAVPAHDQRD FEFARTFGLK IIPVIEGEIS
     EAAFDSKTST CINSSSSEIS INGLDYTSAS SKIISWAESK KIGRKKIQFK LRDWLFARQR
     YWGEPIPLVH YPSGVTKPIP ESELPLVLPN LEEFKPSGTG ESPLALAKDW LQYKDPSTGE
     IGTRETNTMP QWAGSCWYYL RYIDPKNGRF LCDPELEKKW MPVNLYVGGS EHAVLHLLYS
     RFWHKFLFDI GAVSTKEPFD KLIHQGLILG EDKRKMSKSL GNVVNPDDVI KEYGADSLRL
     FEMFMGPLEM VKPWSTRGVE GVFRFLNRIW RLFHSGSQES FRLDDVEPTP EELKILHKTI
     QKVNEDIPNF SFNTAIAQLM IFVNEFTPSD RRPKKVLESF ILLLAPFAPH IAEELWKRSG
     KMESLSYEKF PEADPQYLIE SEILIVVQVN GKLRDEFKAP KDVSQSDAIS MAKNLDKIKG
     ILEGKTIRKE IYVPGKLVNL VIG
//