ID   SYL_LEPBA               Reviewed;         867 AA.
AC   B0SAB8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=LBF_0255;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / Ames;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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; CP000777; ABZ92800.1; -; Genomic_DNA.
DR   RefSeq; WP_012387295.1; NC_010842.1.
DR   AlphaFoldDB; B0SAB8; -.
DR   SMR; B0SAB8; -.
DR   KEGG; lbf:LBF_0255; -.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   OMA; TFMVLAP; -.
DR   BioCyc; LBIF355278:LBF_RS01290-MON; -.
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; -; 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   PANTHER; PTHR43740; PTHR43740; 2.
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; 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..867
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091331"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   867 AA;  99943 MW;  B2315D585FBDB924 CRC64;
     MNYPFQDIEQ KWQKYWDHHQ TFRTNTHSSK PKYYCLDMFP YPSGAGLHVG HPEGYTATDI
     ISRLKRMEGY EVLHPMGWDA FGLPAERYAM TTGIHPRTTT KNNIDTFRRQ IKSLGLSYDW
     EREISTTHPD YYRWTQWIFL QIYNSYFDRK QNKAVPITTL IQTLEREGSL FFEGVELPKG
     IQFTASEWKS KSRKEKEDIL SHFRLVYEAN IPVNWCEALG TVLANEEVEE WTSKGYSVER
     KPMRQYMMRI TAYAERLLND LSLCEWPPST LEMQRNWIGK SEGLELSFHV PSLNKDITVY
     TTRPDTIFGA TYLVLAPEHA LVAELTTPEQ TEAVGQYQKD CSLKSDLERT ELNKDKTGVF
     TGAYAQLPTD PSVKVPIYIS DYVLISYGTG AIMAVPAHDQ RDYDFAVKFN LPIKQVIDGK
     METNLAFDSK DSVCINSSSA EVQLDGKSYK DAFQTMVVWA EKKGIGRKKI QFKLRDWLFA
     RQRYWGEPIP LVHFEDGSPK ALSDSELPLV LPDLEEFKPS GTGESPLALA KDWLVYKDPE
     TGEIGKRETN TMPQWAGSCY YYLRYIDPRN NDKLIDPELE KMWMPVEVYV GGAEHAVLHL
     LYSRFWHKIL FDLGHVSTPE PFKKLVHQGL ILGEDKGKMS KSRGNVVNPD DVVSEFGADT
     LRLFEMFMGP FEMSKPWSKN GVDGVFRFLN RVWRLFHSGE NESFFVEDIE PNEAEQKTLH
     RTIKKVKDDI DSFSFNTAVS QMMIFINEFT SNPRKPKQVL EPFVLALSPF APHLAEELWA
     KLGHTDSLAY HPYPKWDEKY LIDANITIVV QVNGKMRGEF LAPREIEEKE ALSLAKEVEK
     AKPFWVGKEI KKEIYVKGKL VNIVVAG