ID   SYL_MESFL               Reviewed;         801 AA.
AC   Q6F0X5;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 116.
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=Mfl490;
OS   Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS   (Acholeplasma florum).
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC   Entomoplasmataceae; Mesoplasma.
OX   NCBI_TaxID=265311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA   Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA   Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL   Submitted (JUN-2004) 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; AE017263; AAT75848.1; -; Genomic_DNA.
DR   RefSeq; WP_011183388.1; NC_006055.1.
DR   RefSeq; YP_053732.1; NC_006055.1.
DR   AlphaFoldDB; Q6F0X5; -.
DR   SMR; Q6F0X5; -.
DR   STRING; 265311.Mfl490; -.
DR   PaxDb; 265311-Mfl490; -.
DR   EnsemblBacteria; AAT75848; AAT75848; Mfl490.
DR   GeneID; 2898120; -.
DR   KEGG; mfl:Mfl490; -.
DR   PATRIC; fig|265311.5.peg.496; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_14; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000006647; 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; 3.10.20.590; -; 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; 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; 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; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 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; Reference proteome.
FT   CHAIN           1..801
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152041"
FT   MOTIF           39..50
FT                   /note="'HIGH' region"
FT   MOTIF           578..582
FT                   /note="'KMSKS' region"
FT   BINDING         581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   801 AA;  92070 MW;  7B12CCD8B1BCFFD5 CRC64;
     MEFSHKAIEK KWKKYWEENN TNKTTNTSDK KSYVLDMFPY PSGAGIHVGH VKGYTATDVF
     SRYKRMNGYD VLHPMGWDAF GLPAEQYALK TGNDPIDFTL ENIKTFKRQL KMMGFSYDFD
     KEISTANPNY YKITQWIFNQ LYKKGLAENR DVEVNWCQEL GTVLANDEII EKDGLMVSER
     GEHPVTKRKM RQWVLKITEY ADRLLEGLDE LEWNSSIKDL QRNWIGKSTG VELDFLVNNI
     KVPVFTTRID TIYGVSYIVL APEHEQVLNI TTPEQLKEVQ TYIELAKNKS EIDRKDESKP
     KTGVFTGSYA TNPHTNELVQ VWVSDYVLAN YGTGAVMAVP AHDKRDWEFA TKFNLEKKFV
     IENKTDEKAF VGEGKIINSD ILNGMDKKQA IQTMTKIAIE QGWGREQTNY KLRDWLFSRQ
     RFYGEPFPVL YGPNQEITLI EDLPVELPRI KNIKPSGTGE SPLANVEEWV NVEIDGVKYR
     RETNTMPQSA GSSWYYLAYI LADGENEFID IDSAEAKKRF EKWMPVDLYV GGQEHAVGHL
     LYARFWNYVL YDLGITSVKE PFKQLFNQGM ILGPDGRKMS KSWGNVINPD DIVSTHGADS
     LRLYEMFMGP LDASLPWSED GLDSALKWIH RAYRMVMTTE LTDVNDTKLD FVYNDVVKNV
     SEMIESLKFN TAISQLMIFV NAVYKHEGPV YRPYIEGFVK MLSIYAPFIG EELWEKLGHA
     PSITKQAWPV FDPSKLVSNT VVIALQINGK LRATIEVEKG TIKDKLLELA KKQESIISYI
     KDKEIIKEIA VVDRIVNIVI K
//