ID   SYL_MACCJ               Reviewed;         802 AA.
AC   B9E7H4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=MCCL_1435;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH18142.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9E7H4; -.
DR   SMR; B9E7H4; -.
DR   STRING; 458233.MCCL_1435; -.
DR   KEGG; mcl:MCCL_1435; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001383; 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   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
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; PF00133; tRNA-synt_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..802
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199213"
FT   MOTIF           39..50
FT                   /note="'HIGH' region"
FT   MOTIF           574..578
FT                   /note="'KMSKS' region"
FT   BINDING         577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   802 AA;  91101 MW;  456BBFFEAA2D2A37 CRC64;
     MSFNHQTIEK KWQKYWLDNH TFKTTEDKDK NFYALDMFPY PSGAGLHVGH PEGYTATDII
     SRFKRMQGYN VLHPMGWDAF GLPAEQYAID TGNDPAEFTE KNIATFKRQI QELGFSYDWE
     REINTTDPEY YKWTQWIFIQ LYKKGLAYVD EVAVNWCPAL GTVLSNEEVI DGVSERGGHP
     VIRKPMRQWV LKITEYADRL LEDLEELDWP ESLKDMQRNW IGRSEGAEVA FEVENLDHSF
     KVFTTRPDTI YGATYAVLSP EHELVAAITS EEQAEAVKAY QEQAARKSDL ERTDLAKDKT
     GVFTGSYAIN PFNGERMPIW ISDYVLASYG TGAIMAVPAH DERDFEFAKQ FGLDIKPVIE
     GGDNTSAYTG DGAHINSGEL DGLNKEEGIR RAIELLEAKG IGEKKVSYKL RDWLFSRQRY
     WGEPIPVITW EDGSMTTVPE EELPLMLPKT EHIKPSGTGE SPLANIDEFV NVTDPVTGMK
     GRRETNTMPQ WAGSCWYYLR YIDPKNSDMI ADPELLKKWL PVDLYIGGAE HAVLHLLYAR
     FWHKVLYDLG VVHTKEPFQK LFNQGMILGE GNEKMSKSKG NVVNPDDVVA SHGADTLRLY
     EMFMGPLDAS IAWSTNGLDG ARRFLDRVYR LLVNEDGTLS EKITEQPVGS MEKVYHQTVK
     KVTDDYETLG FNTAISQMMV FINEGYKSEQ LNIDHIRGFV KLLNPIAPHI TEELWEKLGG
     TESITYEAWP VYDESKLVDS EVEIVIQVNG KLKQKATIAK DMDKSEMETF ALSLEAVQTA
     IEGKTVRKVI AVPNKLVNIV AN
//