ID   SYL_STRGG               Reviewed;         957 AA.
AC   B1VXF6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=SGR_4973;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(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}.
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DR   EMBL; AP009493; BAG21802.1; -; Genomic_DNA.
DR   RefSeq; WP_012381003.1; NC_010572.1.
DR   AlphaFoldDB; B1VXF6; -.
DR   SMR; B1VXF6; -.
DR   GeneID; 6211000; -.
DR   KEGG; sgr:SGR_4973; -.
DR   PATRIC; fig|455632.4.peg.5086; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   Proteomes; UP000001685; 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   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..957
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091366"
FT   MOTIF           66..77
FT                   /note="'HIGH' region"
FT   MOTIF           728..732
FT                   /note="'KMSKS' region"
FT   BINDING         731
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   957 AA;  106033 MW;  1FF90F2A1C800FB1 CRC64;
     MSETNSAAET AAPHRYTAAM AADIEARWQD FWDAEGTYEA PNPTGDLAGD PELAARPKKF
     IMDMFPYPSG AGLHVGHPLG YIATDVYARH QRMTGHNVLH TLGFDAFGLP AEQYAVQTGT
     HPRVSTEANM ENMKVQLRRL GLGHDNRRSF ATIDSEYYKW TQWIFLQIFN SWYDSEADRA
     RPIAELVEQF ENGTRATPDG REWGALSAAE RADLLSEYRL AYASDAPVNW SPGLGTVLAN
     EEVTADGRSE RGNFPVFKAK LRQWNMRITA YADRLLNDLD GLDWPEAIKL QQRNWIGRSE
     GARVEFPVDT AGGITVFTTR QDTLFGATYM VLAPEHDMVE RIIPAAWPEG THPVWTGGHA
     SPAEAVTAYR KQAAAKSDVE RQAEAKDKTG VFTGAYATNP VSGEKVPVFI ADYVLMGYGT
     GAIMAVPAHD ARDFAFARAF ELPMRCVVQP SDDRGTDPAT WDDAFSSYDA KLVNSANDEI
     SLDGLGVVEA KARITEWLKE HGVGEGTVNF RLRDWLFSRQ RYWGEPFPIV YDEDGIAHPL
     PESMLPLELP EVEDYSPRTF DPEDATAQPE TPLSRNADWV NVTLDLGDGA GPRKYRRETN
     TMPNWAGSCW YELRYLDPNN DRQLVDPSIE QYWMGPREGQ PTGGVDLYVG GAEHAVLHLL
     YARFWSKVLH DLGHISSAEP FHKLYNQGMI QAFVYRDSRG IAVPAAEVEE RDGAFYHAGE
     KVSRVLGKMG KSLKNAVTPD EICAEYGADT LRLYEMAMGP LDVSRPWDTR AVVGQYRLLQ
     RLWRNVVDEA TGEVTVVDTE PDEDTLRALH KAIDGVGQDM AGMRFNTAIA KVTELNNHLT
     KAGGPLSRSV AERLVLLIAP LAPHIAEELW RRLGHADSVV HQDFPVADPA YVVDETVTCV
     VQIKGKVRAR LEISPAITDE ELEALALADE AVVAALGGAG IRKVIVRAPK LVNIVPA
//