ID   SYL_PARUW               Reviewed;         845 AA.
AC   Q6MCC8;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=pc1047;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
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; BX908798; CAF23771.1; -; Genomic_DNA.
DR   RefSeq; WP_011175597.1; NC_005861.1.
DR   AlphaFoldDB; Q6MCC8; -.
DR   SMR; Q6MCC8; -.
DR   STRING; 264201.pc1047; -.
DR   EnsemblBacteria; CAF23771; CAF23771; PC_RS05045.
DR   KEGG; pcu:PC_RS05045; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000529; 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; Reference proteome.
FT   CHAIN           1..845
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152058"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           623..627
FT                   /note="'KMSKS' region"
FT   BINDING         626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   845 AA;  97641 MW;  518041736EAB1249 CRC64;
     MKYDHQQIEA KWQKFWQDNQ TYRSDDNFQK PKYYVLDMFP YPSGAGLHVG HVVGYTATDI
     IARYMRTKGY NVMHPMGWDS FGLPAEQYAI RTGTHPAEST QENINNYRRQ LRALGFSYDW
     NRELATSDPN YYKWTQWIFT KLYEKGLAYE AEMLVNYCPA LGTVLANEEI ENGKTKDGGH
     PVERRPLKQW ILKITAYADR LLQDLDLLDW PESLKKLQIN WIGKSEGAYV QFIEKTTQEA
     FSVFTTRPDT LFGVSYLVLA PEHPLVSHIT ASSQQQAVRA YQAQIASKSD LDRTELNRDK
     TGVFTGAYAV NPVNHKEIPI WISDYVLMNV GTGAIMAVPA HDERDFEFAK TFKLPIIPVY
     DPVCEEITIR NQVLAGQQCW PGHGICVNSA CGDLSLNGLN LDQAKKIVIN WLEINHKGKS
     ATTYKLRDWL FSRQRYWGEP FPLLKFEDGS VRLLDEDELP LCPPAITNYK PTGDGKGPLT
     QIKEWVEIID TKTGKKAFRD TNIMPQWAGS CWYYLRFCDP HNTEKAFSPE KEKYWLPVDL
     YIGGVEHAVL HLLYARFWHK VLYDCGYVHT LEPFQTLRNQ GLVVARSYQN KMRVYVEPRY
     VEQRDGKYFD SRTGEELTSQ IDKMSKSKLN GESPDEIIQE YGADALRLYE MFMGPLEKEK
     VWNTDAVSGT RRFLNRFYEM AFSDKVTNET SEEGLKLGHR LVHSVMKDME LLQFNTAIAK
     MMEFINEFTK LVTYPKQVIQ MATQVLAPFA PHLAEEVWEH LKCEGSLSFT PYPQVEEKYL
     QENVITYVVQ INGKVRGRFD LPKDQTQENV LEAAKNNPHI QQYINKKEIG KVVFVPNKLL
     SIVLR