ID   SYL_CHLT2               Reviewed;         819 AA.
AC   B0B9V9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=CTL0461;
OS   Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=434/Bu / ATCC VR-902B;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(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; AM884176; CAP03900.1; -; Genomic_DNA.
DR   RefSeq; WP_009873640.1; NC_010287.1.
DR   RefSeq; YP_001654537.1; NC_010287.1.
DR   AlphaFoldDB; B0B9V9; -.
DR   SMR; B0B9V9; -.
DR   EnsemblBacteria; CAP03900; CAP03900; CTL0461.
DR   KEGG; ctb:CTL0461; -.
DR   PATRIC; fig|471472.4.peg.496; -.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000795; 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..819
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091305"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           600..604
FT                   /note="'KMSKS' region"
FT   BINDING         603
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   819 AA;  92846 MW;  7F059DFDF9BBA128 CRC64;
     MRYDPGLIEE KWQKFWKNEQ VFKAEEDETK TKYYVLDMFP YPSGAGLHVG HLIGYTATDI
     VARCKRAQGF SVLHPMGWDS FGLPAEQYAI RTGTHPRETT EKNIANFKKQ LTAMGFSYDE
     SREFATSDPE YYKWTQKLFL ILYEKGLAYM ADMAVNYCPE LGTVLSNEEI ENGFSVDGGY
     PVERRMLRQW VLRITAFADQ LLEGLDELDW PESVKQLQKN WIGKSSGASV NFATEHGAIE
     VFTTRPDTLI GVSFLALAPE HPLVDLLTSD EQKAVVAQYI KETQSKSERD RISEMKTKSG
     VFTGSYAKHP VTHELIPIWI ADYVLMGFGS GAVMGVPAHD ERDLLFAEQF NLPVVSVLNE
     EGVCINSCCE GFHLDGLSGE EAKQYVINFL EENHLGAAKI AYKLRDWLFS RQRYWGEPIP
     IIHFEDGSCR PLRDDELPLL PPEIQDYRPE GVGQGPLAKV REWVQVFDTE TQRAGKRETH
     TMPQWAGSCW YYLRFCDAHN SAAPWAKEKE QYWMPVDLYI GGAEHAVLHL LYARFWHQVF
     YEAGIVSTPE PFKKLVNQGL VLATSYRIPG KGYIYPETAK EENGKWVAPS GEELDVRQEK
     MSKSKLNGVD PQILIDEFGA DAVRMYAMFS GPLDKNKLWS NQGVAGCRRF LNRFYEMVSS
     DRVKEDNNFE GLSLAHKLVQ RVTDAIEKLS LNTIPSSFME FINDFVKLAV YPKSAVEMAV
     RALAPIAPHI SEELWVLLGN SPGVQKSGWP SVLPEYLEEQ TVTIVVQVNG KLRARLDIMK
     DASKEEVLAL ARESASKYLE GCEVKKAIFV PARLVNFVV