ID   SYL_MYCMM               Reviewed;         976 AA.
AC   B2HIA2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=MMAR_0057;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000854; ACC38528.1; -; Genomic_DNA.
DR   RefSeq; WP_012392063.1; NC_010612.1.
DR   AlphaFoldDB; B2HIA2; -.
DR   SMR; B2HIA2; -.
DR   STRING; 216594.MMAR_0057; -.
DR   EnsemblBacteria; ACC38528; ACC38528; MMAR_0057.
DR   KEGG; mmi:MMAR_0057; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001190; 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   Gene3D; 3.90.740.10; -; 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   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..976
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091336"
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;  107116 MW;  3848111BF66E48F7 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 AAYRRAIAAK SDLERQESKE KTGVFLGSHA
     INPATGQPVP IFIADYVLAG YGTGAIMAVP GHDQRDWDFA RALGLPVVEV IAGGDISQAA
     YTGDGVLVNS GFLDGMSVGE AKQAITARLE SDGHGQARIE FKLRDWLFAR QRYWGEPFPI
     VYDADGRPHA LDESALPVEL PDVPDYSPVL FDPDDANSEP SPPLGKATEW VHVELDLGDG
     LKPYSRDTNV MPQWAGSSWY ELRYTDPHNA DRFCAKENET YWMGPRPAEH GPDDPGGVDL
     YVGGAEHAVL HLLYARFWHK VLYDLGHVSS REPYRKLINQ GYIQAFAYTD ARGSYVPAEE
     VIERDGGFVY PGADGEIEVF QEFGKIGKSL KNSISPDEIC DDYGADTLRV YEMSMGPIEA
     SRPWATKDVI GAYRFLQRVW RLVIDENTGE ILVADTPAEL DTDTLRALHR AIAGVAEDYA
     ALRNNTAVAK LIEYTNFLTK RHRDAVPRAA IEPLVLMVAP LAPHLAEELW QRLGHTTSLA
     HGPFPAADPA YLIDDTVEYP VQVNGKVRGR VVVAADADDD AVKAAALADE KVQAFLAGAS
     PRKVIVVAGR LVNLVV