ID   SYL_TREPS               Reviewed;         878 AA.
AC   B2S3H7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=TPASS_0586;
OS   Treponema pallidum subsp. pallidum (strain SS14).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=455434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS14;
RX   PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA   Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA   Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA   Molla M.N., Albert T.J., Weinstock G.M.;
RT   "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT   determined with oligonucleotide arrays.";
RL   BMC Microbiol. 8:76-76(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; CP000805; ACD71006.1; -; Genomic_DNA.
DR   RefSeq; WP_010882032.1; NC_021508.1.
DR   AlphaFoldDB; B2S3H7; -.
DR   SMR; B2S3H7; -.
DR   EnsemblBacteria; ACD71006; ACD71006; TPASS_0586.
DR   KEGG; tpp:TPASS_0586; -.
DR   PATRIC; fig|455434.6.peg.583; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001202; 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; 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; 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.
FT   CHAIN           1..878
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199232"
FT   MOTIF           43..54
FT                   /note="'HIGH' region"
FT   MOTIF           634..638
FT                   /note="'KMSKS' region"
FT   BINDING         637
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   878 AA;  98991 MW;  DCD74E2DC3652B74 CRC64;
     MGYPFRALEK KWQAYWRDKR VFCVSEDERF PPERRAYVLD MFPYPSAQGL HVGHPEGYTA
     TDIYCRYLRM GGYNVLHPMG FDAFGLPAEN FALKTGTHPR VSTSANCDTF RRQIQSFGFS
     YDWEREISTA DPEYYRWTQW LFLKLYEKGL AYEATAPINW CPSCKTGLAN EEVRDACCER
     CGAEVTRRGV RQWMVRITAY AERLLSDLDE LDWPESVKQM QRNWIGKSCG AEIDFPVDAP
     ACSVHDKLPQ TIRVYTTRAD TLFGVTYLVL APEHEAVTAL TTHAQRAAVQ AYVQRAAKKN
     DLERTDLAKE KTGVFTGAYV RNPINDMRIP VWVGDYVLVS YGTGAVMAVP AHDQRDWDFA
     TRFGLPKLTV VSADYTATVP NSNSPQGAVL QRCVSDEGFV VNSGAFNGLA SADARERIVA
     HLEMRGAGAR RVTYRLRDWV FSRQRYWGEP IPLVHCPSCG VVPLPESALP LLLPETADFT
     PTEDGQGPLA RARTWLRVPC PQCASDAVRE TNTMPQWAGS CWYYLRYMDP RNKTAFCAPE
     KERYWAPVAL YVGGAEHAVL HLLYARFWHK VLYDLGLVST KEPFARLVNQ GMITSYAYRR
     KNGALVPHDE VHTNAQGTYV HARTGEKLEC VVAKMSKALK NVVNPDDMIA AYGADACRVY
     EMFMGPLEAS KPWNTQGLVG VFRFLEKIWV LAGRVAAANG IPQDSRAEPP GDLHAQKKSC
     SMYALETLLH RTIQKVTDDT SALSFNTAIS QMMIFVNEAT RVARRMPLPS KMWEMFVKIL
     SPYAPHLAEE LWEMCGHTHT IAYEPWPQVD PARVAPHVCS VVVQVNGKVR DTFSVAPNAP
     NEELEQKARE TAGARKFLGT QQPKRVVIVP NKLVNFVL