ID   SYL_TREPA               Reviewed;         878 AA.
AC   O83595;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 143.
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=TP_0586;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC65562.1; -; Genomic_DNA.
DR   PIR; C71305; C71305.
DR   RefSeq; WP_010882032.1; NC_021490.2.
DR   AlphaFoldDB; O83595; -.
DR   SMR; O83595; -.
DR   IntAct; O83595; 24.
DR   STRING; 243276.TP_0586; -.
DR   EnsemblBacteria; AAC65562; AAC65562; TP_0586.
DR   KEGG; tpa:TP_0586; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_12; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000811; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   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; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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..878
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152109"
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
//