ID   SYL_LEPBL               Reviewed;         864 AA.
AC   Q054T5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=LBL_0571;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=355276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L550;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000348; ABJ78160.1; -; Genomic_DNA.
DR   RefSeq; WP_011669510.1; NC_008508.1.
DR   AlphaFoldDB; Q054T5; -.
DR   SMR; Q054T5; -.
DR   KEGG; lbl:LBL_0571; -.
DR   HOGENOM; CLU_004427_0_0_12; -.
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; 3.40.50.620; HUPs; 3.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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.
FT   CHAIN           1..864
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009365"
FT   MOTIF           40..51
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   864 AA;  99488 MW;  15A6F0DFD8404D54 CRC64;
     MQYPFQEVES FWQKFWEENK SFQTNIRSSK PKFYCLDMFP YPSGAGLHVG HPEGYTATDI
     LSRFKRMKGF EVLHPMGWDA FGLPAERYAM QTGIHPAITT KNNIDNFRRQ IQMIGLSYDW
     SRELSTTDPD YYKFTQWIFI QLYQSWFNPE LKKAESIETL IQRFSNKGSA DLDYKPFSAQ
     EWKQFSLVEK EKILSDFRLV YQAEIPVNWC EALGTVLANE EVEEWIDKGY EVVRKPMRQY
     MMRITAYADR LLEDLKLVQW PSSTLEMQKN WIGKSEGLEI TFPFKKPLKS GSDGIRIFTT
     RPDTIFGVTY MVVAPEHPIV SEITTPEQKQ KVEEYQKVSS LKSDLDRMEL TKEKTGVFTG
     SFVLNPANPS KEIPIWISDY VLYGYGTGAI MAVPAHDQRD YEFAKTFGLE ILPVIEGEIT
     DVAFDSKTSI CIHSSSSEIS IDGLDYSSAS SKIISWAESK RIGKKKTQFK LRDWLFARQR
     YWGEPIPLVH YPSGITKPIP ESELPLELPP NLEEFKPSGT GESPLALAKE WLQYKDPETG
     EIGTRETNTM PQWAGSCWYY LRYIDPKNGK LFCDPDLEKK WMPVDLYVGG AEHAVLHLLY
     SRFWHKFLYD IGVVSTQEPF AKLIHQGLIL GEDKRKMSKS LGNVINPDDV IRKYGADSLR
     LFEMFMGPLE MVKPWSTRGV EGVFRFLNRV WRLFHTGEGE SFRLDEIEPT TEELKILHKT
     IQKVGEDIPN FSFNTAISQL MIFVNEFTPS DRRPKEVLET FILLLAPFAP HIAEELWKRS
     GNNKSLSTEK FPEADPQYLV ESEILIVVQV NGKLRDEFKA PKDVSEADAI SIAKNLDKIK
     GILDGKTIRK EIYVPGKLIN LVIG
//