ID   SYL_CHLMU               Reviewed;         819 AA.
AC   Q9PKI4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 138.
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=TC_0481;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39327.1; -; Genomic_DNA.
DR   PIR; G81698; G81698.
DR   RefSeq; WP_010230558.1; NZ_CP063055.1.
DR   AlphaFoldDB; Q9PKI4; -.
DR   SMR; Q9PKI4; -.
DR   GeneID; 1245839; -.
DR   KEGG; cmu:TC_0481; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000800; 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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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_0000151997"
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;  93015 MW;  024D7E1BD2E900B4 CRC64;
     MRYDPSLIEE KWQKFWKEEQ TFRAEEDETK TKYYVLDMFP YPSGAGLHVG HLIGYTATDI
     VARYKRAKGF SVLHPMGWDS FGLPAEQYAI RTGTHPRETT EKNIANFKQQ LTSMGFSYDE
     SREFATSDPE YYKWTQKLFL ILYEKGLAYM ADMAVNYCPE LGTVLSNEEV ENGFSVEGGY
     PVERRMLRQW VLRITAFADQ LLGGLDELDW PESVKQLQRN WIGKSVGASV HFETEHGVLE
     VFTTRPDTLI GVSFLVLAPE HPLVDLLTSD EQKTIVAQYV KETQSKSERD RISEMKTKSG
     VFTGAYAKHP VTQNPIPIWI ADYVLMGYGS GAVMGVPAHD DRDLLFAQQF DLPIISVVSE
     DGVCINSCHE DFSLDGLSGE EAKQYVINFL EKNNLGSAKV AYKLRDWLFS RQRYWGEPIP
     VIHFEDGSCR PLKDDELPLL PPEIQDYRPE GVGQGPLAKV KEWVNVFDSE TQKEGKRETH
     TMPQWAGSCW YYLRFCDAHN SCAPWAEEKE QYWMPVDLYI GGAEHAVLHL LYARFWHQVF
     YEAGIVSTPE PFKKLVNQGL VLSTSYRIPG KGYIAPEMAK EENGQWISPS GELLDVRQEK
     MSKSKLNGVD PKVLIDEFGA DAVRMYAMFS GPLDKNKLWS NQGVAGCRRF LNRFYEMATS
     SRVKDEDIFE GMSLAHKLVQ RVTDDIEKLS LNTITSSFME FINEFVKLPV YPKNAVEMAV
     RALAPIAPHI SEELWVLLGN ASGIEKAGWP KALPEYLEGK IVTIVVQVNG KLRARLDISK
     DAIEEEVVAL AKEAVSKYLE GGVVRKTIFV LNRLVNFVI
//