ID   SYL_MYCUA               Reviewed;         976 AA.
AC   A0PKG2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=MUL_0056;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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; CP000325; ABL02831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0PKG2; -.
DR   SMR; A0PKG2; -.
DR   KEGG; mul:MUL_0056; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   Proteomes; UP000000765; 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   Gene3D; 3.40.50.620; HUPs; 3.
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..976
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009376"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           86..97
FT                   /note="'HIGH' region"
FT   MOTIF           745..749
FT                   /note="'KMSKS' region"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         748
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   976 AA;  107185 MW;  42E0040F495963EA CRC64;
     MTESPTTTPG STSGAPSGVP SGVNDAESDA PRHRYTAELA AGVERTWQQN WARLGTFNVP
     NPVGSLAPSD GSPVPEDKLF VQDMFPYPSG EGLHVGHPLG YIATDVFARY HRMKGRNVLH
     ALGFDAFGLP AEQYAVQTGT HPRTRTEANV VNFRRQLGRL GLGHDSRRSF STTDVEFYKW
     TQWIFLQIYN AWFDAAANKA RPISELVAEF DSGARSLVDG RDWSTLSAGE RADVIDDHRL
     VYRADSMVNW CPGLGTVLAN EEVTSDGRSD RGNFPVFRKR LRQWMMRITA YSDRLLDDLD
     VLDWPDQVKT MQRNWIGRST GASALFTATR SNGETVGLEV FTTRPDTLFG ATYLVLAPEH
     DLVDDLVGAG WPAGVDPLWT GGGATPAEAV AAYRRAIAVK SDLERQESKE KTGVFLGSHA
     INPATGQPVP IFIADYVLAG YGTGAIMAVP GHDQRDWDFA RALGLPVVEV IAGGDISQAA
     YTGDGVLVNS GFLDGMSVGE AKQAITARLE SDGYGQARIE FKLRDWLFAR QRYWGEPFPI
     VYDADGRPHA LDESALPVEL PDVPDYSPVL FDPDDANSEP SPPLGKATEW LHVELDLGDG
     LKPYSRDTNV MPQWAGSSWY ELRYTDPHNA DRFCAKENET YWMGPRPAEH GPDDPGGVDL
     YVGGAEHAVL HLLYARFWHK VLYDLGHVSS REPYRKLINQ GYIQAFAYTD ARGSYVPAEE
     VIERDGGFVY PGADGEIEVF QEFGKIGKSL KNSISPDEIC DDYGADTLRV YEMSMGPIEA
     SRPWATKDVI GAHRFLQRVW RLVIDENTGE ILVADTPAEL DTDTLRALHR AIAGVAEDYA
     ALRNNTAVAK LIEYTNFLTK RHRDAVPRAV IEPLVLMVAP LAPHLAEELW QRLGHTTSLA
     HGPFPAADPA YLIDDTVEYP VQVNGKVRGR VVVAADADDD AVKAAALADQ KVQAFLAGAS
     PRKVIVVAGR LVNLVV
//