ID   SYL_CHLTA               Reviewed;         819 AA.
AC   Q3KMF3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=CTA_0229;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX50469.1; -; Genomic_DNA.
DR   RefSeq; WP_011324641.1; NC_007429.1.
DR   AlphaFoldDB; Q3KMF3; -.
DR   SMR; Q3KMF3; -.
DR   KEGG; cta:CTA_0229; -.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   Proteomes; UP000002532; 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.
FT   CHAIN           1..819
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009323"
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;  92890 MW;  85B2C1D116E8AB5D CRC64;
     MRYDPGLIEE KWQKFWKNEQ VFKAEEDETK TKYYVLDMFP YPSGAGLHVG HLIGYTATDI
     VARYKRAQGF 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 ADYVLIGFGS GAVMGVPAHD ERDLLFAEQF NLPVVSVLNK
     EGVCINSCCE GFHLDGLSGE EAKQYVINFL EENHLGAAKI AYKLRDWLFS RQRYWGEPIP
     IIHFEDGSCR PLRDYELPLL PPEIQDYRPE GVGQGPLAKV REWVQVFDTE TQRAGKRETH
     TMPQWAGSCW YYLRFCDAHN SAAPWAKEKE QYWMPVDLYI GGAEHAVLHL LYARFWHQIF
     YEAGIVSTPE PFKKLVNQGL VLATSYRIPG KGYIYPEIAK EENGKWVAPS GEELDVRQEK
     MSKSKLNGVD PQILIDEFGA DAVRMYAMFS GPLDKNKLWS NQGVAGCRRF LNRFYEMVSS
     DRVKEDNNFE GLSLAHKLVQ RVTDAIEKLS LNTIPSSFME FINDFVKLAV YPKSAVEMAV
     RALAPIAPHI SEELWVLLGN SPGVQKSGWP SVLPEYLEGQ TVTIVVQVNG KLRARLDIMK
     DASKEEVLAL ARESASKYLE GCEVKEAIFV PARLVNFVV
//