ID   SYL_SACEN               Reviewed;         955 AA.
AC   A4FR54;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SACE_7373;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(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; AM420293; CAM06529.1; -; Genomic_DNA.
DR   RefSeq; WP_009945755.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FR54; -.
DR   SMR; A4FR54; -.
DR   STRING; 405948.SACE_7373; -.
DR   EnsemblBacteria; CAM06529; CAM06529; SACE_7373.
DR   KEGG; sen:SACE_7373; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000006728; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..955
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334809"
FT   MOTIF           66..77
FT                   /note="'HIGH' region"
FT   MOTIF           725..729
FT                   /note="'KMSKS' region"
FT   BINDING         728
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   955 AA;  107406 MW;  37394D241D975782 CRC64;
     MSGQAEGSTN TEEVPRFRYT AQTAAEIEQR WQRRWEELGT FHAPNPAGSL KGEVSDEKLF
     VQDMFPYPSG SGLHVGHPLG FIGTDVYARF NRMLGKNVLH TMGFDSFGLP AEQYAVQTGT
     HPRTTTEKNI ERYLTQIRRL GLGHDERRRV ATTDIPFYRW TQWIFLQIFH SWYDTDADRA
     RPISELEAQF AAGERATPDG RPWAELSRTE QRRIIDSYRL VYLSEAPVNW APGLGTVVAN
     EEVTADGLTE RGNFPVFRRN LKQWMMRITA YADRLIDDLD RLDWPDKIKT MQRNWIGRSQ
     GANVVFPLDG SAGSIEVFTT RPDTLFGVTY LVLAPEHPLV DELTAAQWPQ DPDLRWTGGA
     ATPAEAVAQY RRAASMKSDL DRQENKEKTG VFTGAWATNP VNGEQVPVFI ADYVLMGYGT
     GAIMAVPGED QRDFDFAEAF GLPVVRTVQP SEGFEGGAYS GEGPRINSAN PDVGLDLNGM
     HLDEAKKTII EWLESHKHGS GTVQYKLRDW LFARQRYWGE PFPVVYDSDG IPLGLPESEL
     PVVLPEVADY SPRTFDPEDA DSRPEPPLAK ATEWANVELD LGDGLKNYER DTNVMPQWAG
     SCWYQLRYID PDNDQAFVDP ANERYWMGKR PELHGPDDPG GLDLYIGGVE HGVLHLLYSR
     FWHKVLYDLG HVSSEEPYRR LYNQGYIQAY AYTDSRGVYV PAEEVEERDG KFFFQGEEVR
     REYGKMGKSL KNSVSPDEMA DAYGADTLRL YEMAMGPLDA SRPWATKDVV GSHRFLQRLW
     RNVVDENTGE LRVTDDEPAI EVLRALHKTI AGVREDYREL RFNTAVAKLI ELNNLLTKEY
     SATGAPRAVV GPLVLMVAPL APHMAEELWS KLGHDGSLAH GPFPEADEQY LVEDTVEYPI
     QFNGKVRSRI VVPASAGQDE VKAAALADEK VVAALDGREP RKVIVVPGRL VNVVG