ID   SYL_SALTO               Reviewed;         954 AA.
AC   A4X9S8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Strop_3225;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(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; CP000667; ABP55659.1; -; Genomic_DNA.
DR   RefSeq; WP_012014436.1; NC_009380.1.
DR   AlphaFoldDB; A4X9S8; -.
DR   SMR; A4X9S8; -.
DR   STRING; 369723.Strop_3225; -.
DR   EnsemblBacteria; ABP55659; ABP55659; Strop_3225.
DR   KEGG; stp:Strop_3225; -.
DR   PATRIC; fig|369723.5.peg.3317; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000235; 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; -; 3.
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..954
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091362"
FT   MOTIF           67..78
FT                   /note="'HIGH' region"
FT   MOTIF           729..733
FT                   /note="'KMSKS' region"
FT   BINDING         732
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   954 AA;  106010 MW;  46A367CA446A4CB6 CRC64;
     MTEAAAPASD IPPFRYTADL ADEIERRWQD TWEREGTFHA PNPTGPLADP EHPRAGAEKL
     YVLDMFPYPS GAGLHVGHPL GYIGTDCFAR YQRMAGRNVL HAMGFDAFGL PAEQYAVQTG
     THPRTTTEAN IARYKAQLRR LGLAHDERRS VATIDADFYR WTQWVFLQIY NAWYDSSAKR
     ARPIAELVAE FSGGSRRTPD GRPWGELTDA ERRAVVDQHR LAYVSQAPVN WCPGLGTVLA
     NEEVTADGRS ERGNFPVFKR NLKQWMMRIT AYGDRLLDDL EKLDWPEPIK LMQRNWIGRS
     TGAHIEFPTS APDSDAEGEP RISVFTTRPD TIFGATYLVL APEHDLVDTL VPTAWPAGVP
     QAWTGGQASP REAVAGYRKV AAAKTDLERQ AETKEKTGVF IGSYATNPVT GAQIPIFIAD
     YVLAGYGTGA IMAVPGQDER DWAFAEVFDL PIVRTVQPAE GFAGKAYTGD GLAINSATPE
     RGLDLNGLGV AEAKARTIAW LEAGGHGSGA VTYRLRDWLF SRQRYWGEPF PIVYDETGAA
     IALPEELLPV ELPEVDDFAP RTFDPSDAES NPETPLSRRR DWVEVELDLG DGPKRYTRET
     NVMPQWAGSC WYELRYLDPT NGDRFVDPEA ERYWMGPRGE GDCGGTDLYV GGAEHAVLHL
     LYARFWHKVL YDLGHVSSFE PFRKLFNQGY IQAYAYTDAR GAYVPAEEVV ERSGTYYLGD
     VQVNREYGKM GKSLRNVVTP DEMCAAYGAD TFRVYEMSMG PLEVSRPWET RAVVGSFRFL
     QRVWRAIVDE RSGASRVVDV PADEATRRLL HRIVDGVRGD MEAMRFNTTI AKLIELTNAL
     TRLPETPREV AEPLVLMLAP FAPHVAEELW RRMGHETSLT YADFPVADPA LLVAESVTYP
     VQVNGKVRGR IEVPADAGQE TVRAAALEAV AASLAGKEPR KVIVVPGRMV SVVA