ID   SYL_MYCPA               Reviewed;         969 AA.
AC   Q744V3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 121.
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=MAP_0048;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS02365.1; -; Genomic_DNA.
DR   RefSeq; WP_003876813.1; NZ_CP106873.1.
DR   AlphaFoldDB; Q744V3; -.
DR   SMR; Q744V3; -.
DR   STRING; 262316.MAP_0048; -.
DR   KEGG; mpa:MAP_0048; -.
DR   PATRIC; fig|262316.17.peg.52; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   Proteomes; UP000000580; 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; Reference proteome.
FT   CHAIN           1..969
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152048"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           78..89
FT                   /note="'HIGH' region"
FT   MOTIF           737..741
FT                   /note="'KMSKS' region"
FT   BINDING         740
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   969 AA;  106918 MW;  C1D2A396E4833CA2 CRC64;
     MTESPTTSPA TGSGAAAPDS DAPPYRYTAA LAGRIEGSWQ DTWAKLGTFN VPNPVGSLAP
     TDGTPVPEDK LFVQDMFPYP SGEGLHVGHP LGYIATDVYA RYFRMTGRNV LHALGFDAFG
     LPAEQYAVQT GTHPRTRTEA NVVNFRRQLG RLGLGHDSRR SFSTTDVEFY KWTQWIFLQI
     YNAWFDPAAN KARPIAELVA EFDSGARSLD DGRNWSELSA GERADVIDSH RLVYRADSMV
     NWCPGLGTVL ANEEVTADGR SDRGNFPVFR KRLRQWMMRI TAYSDRLLDD LDLLDWPEPV
     KTMQRNWIGR STGAKALFAA TGADGAALDI EVFTTRPDTL FGATYMVLAP EHELVDELVA
     PAWPDGTDPR WTYGAATPGE SVAAYRRAIA SKSDLERQES KAKTGVFLGS YATNPTNGKP
     VPIFIADYVL AGYGTGAIMA VPGHDQRDWD FAHEFGLPIV EVIAGGDISE GAYAGDGVLV
     NSGYLDGLDV AAAKEAITAR LEAEGRGCAR VEYKLRDWLF ARQRYWGEPF PIVYDSDGRP
     HALDEAALPV ELPDVPDYSP VLFDPDDADS EPSPPLAKAT DWVHVELDLG DGLKPYSRDT
     NVMPQWAGSS WYELRYTDPH NSERFCAKEN EAYWMGPRPA EHGPQDPGGV DLYVGGAEHA
     VLHLLYARFW HKVLYDLGHV SSREPYRRLV NQGYIQAFAY TDSRGSYVPA EEVVERDGRF
     FYRGPDGEIE VFQEFGKIGK SLKNSISPDE ICDDYGADTL RVYEMSMGPL EASRPWATKD
     VVGAHRFLQR VWRLVVDEQT GETRVVDGAG RDLPTGTLRL LHRTIAGVSE DYAALRNNTA
     VAKLIEYTNH LTKEHRDAVP RAAVEPLVLM LAPLAPHMAE ELWLRLGHTT SLAHGPFPVA
     DPAYLVEDTV EYPVQVNGKV RGRVTVAADA DRDTLEAAAL ADEKVLAFLA GAQPRKVIVV
     PGRLVNLVV
//