ID   SYL_LAWIP               Reviewed;         835 AA.
AC   Q1MS17;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=LI0152;
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00;
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) 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; AM180252; CAJ54208.1; -; Genomic_DNA.
DR   RefSeq; WP_011526235.1; NC_008011.1.
DR   AlphaFoldDB; Q1MS17; -.
DR   SMR; Q1MS17; -.
DR   STRING; 363253.LI0152; -.
DR   KEGG; lip:LI0152; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002430; 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   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; Reference proteome.
FT   CHAIN           1..835
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334768"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT   MOTIF           587..591
FT                   /note="'KMSKS' region"
FT   BINDING         590
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   835 AA;  96315 MW;  98E033A6AB677868 CRC64;
     MIMHSNYDPN IIEKKWQRYW EEQHAYACDI DPNKKKYYVL EMWPYPSGNI HMGHVRNYSI
     GDVIARIKRM QGYNVLHPMG WDAFGLPAEL AAIKHHTQPA DWTYTNINEM RAQLKRLGYS
     YDWQREIATC DPDYYQWEQL FFVDCFEKGL VYRKKAPQNW CPSCNTVLAN EQVIEGSCWR
     CDTSIIQKEL TQWFLKITDY AEELLDDLTT LKYSWPDRVI TMQENWLGKS TGVEISFPIE
     SSQDFITIFT TRPDTIFGAT AIILAPEHPI LETLLNDTPQ KEKLYNVIEK MRNMDRLERQ
     SNLLTKEGIF IDRYCINPCS GDKIPIWIGN FVLADYGTGA IMAVPAHDQR DFDFCKKYNL
     PISIVIQPDE LQINEHTIVE PWTGLGTLIH SGQFTGLTNK EAKEKITQYL EKIGKATRVV
     SWRLRDWNIS RQRYWGTPIP IIYCKNCGVV SVPKNELPVI LPTNITINED GSSPLPQESS
     FIDCMCPQCG GIAKRETDTM DTFVDSSWYF ARFVDPKNTK QPFDTSIAKY WLNVDQYIGG
     VEHAILHLLY SRFFTKLLRD LGYLPSNINE PFAKLLTQGM VIKDGSKMSK SKGNIVDPNQ
     MINIYGADTI RLFCLFAAPP ERDFDWSDSG IEGSYRFLHR VWRLFIDVQP HIHTTHAGNS
     TVIETTTALT KDVKRKEHIT IKKVSEDIEN KYQFNTAIAS IMEFVNTLYL SKNELILTVE
     GKNILSSAIA TVLTLLSPMT PHICEELWSY LGHSTSISLE PWPKWDPQAL LKDVVTIVVQ
     INGKVRNKFE VPMDLSKEEL EHIIFNDTKI TQYLEGKTIQ KHIIIPNKII NIVTT