ID   SYL_MYCCT               Reviewed;         804 AA.
AC   Q2SRI9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=MCAP_0659;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000123; ABC01150.1; -; Genomic_DNA.
DR   RefSeq; WP_011387520.1; NC_007633.1.
DR   AlphaFoldDB; Q2SRI9; -.
DR   SMR; Q2SRI9; -.
DR   EnsemblBacteria; ABC01150; ABC01150; MCAP_0659.
DR   GeneID; 23778386; -.
DR   KEGG; mcp:MCAP_0659; -.
DR   HOGENOM; CLU_004427_0_0_14; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   PhylomeDB; Q2SRI9; -.
DR   Proteomes; UP000001928; 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; IPR002300; aa-tRNA-synth_Ia.
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; PF00133; tRNA-synt_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..804
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009374"
FT   MOTIF           39..50
FT                   /note="'HIGH' region"
FT   MOTIF           580..584
FT                   /note="'KMSKS' region"
FT   BINDING         583
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   804 AA;  92983 MW;  C96DDA009800B974 CRC64;
     MDFSHKAIEK KWQKYWKENN VYKTTDSNHK KAYVLDMFPY PSGAGLHVGH IKGYTATDVY
     SRFKRMQGYD VLHPIGWDAF GLPAEQYALK TGNDPRDFTL KNIENFKAQL VKMGFSYDYD
     KEINTADPNY YKVTQWIFKE LYKKGLAENR NIDVNWCQEL GTVLANDEII EKDGLMVSER
     GEYPVVKKKM RQWVLKITDY ADKLLKGLDN LDWPNSVKEL QRNWIGKSEG CEINFKSNDI
     NIPVFTTRAD TVFGATYIVL APENELVLKL TTPNKLDEVK KYIELTANKS EIERKDESKT
     KTGVFIGSYA INPLTKEQIQ IWISDYVLND YGSGAIMAVP AHDKRDWDFA TKFNLPIRFV
     ISTKDESKAF VGEGKHINSE FLNDLDRIQS LQVIHDYIEK NNLGKKKTNY KLRDWLFSRQ
     RFYGEPFPVL YDKDNNIILV EDDDLPITLP KTDYIKPTNT GESPLANVKN WVNVKIGDRE
     YKRETNTMPQ SAGSSWYFIA YILANSKNNL IDLTSDEAKK RLEKWLPVDL YIGGQEHAVG
     HLLYSRFWTH FLYDLGLLPT SEPFQRLFNQ GMILGPDNRK MSKSWGNVIN PDDVIDTHGA
     DALRLYEMFM GPLDASLPWS FDGLDASLKW LNRCYRMINK IEFSNTNNHK LDYVYNDVVK
     KVTQMITELK FNTAISQLMV LVNAIYKEEL STVYKPYIEG FVKMLSLFSP HLAEELWEKL
     GNNSSVTLQA WPEFDETKIV KNTVVIALQV NGKLRSTIEV EKGTDKETLI KLAQENENII
     RFIKGHKNLK YIAVVDRIVN IVIE