ID   SYL_CORJK               Reviewed;         976 AA.
AC   Q4JSF0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 132.
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=jk2075;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(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; CR931997; CAI38257.1; -; Genomic_DNA.
DR   RefSeq; WP_005292496.1; NC_007164.1.
DR   AlphaFoldDB; Q4JSF0; -.
DR   SMR; Q4JSF0; -.
DR   STRING; 306537.jk2075; -.
DR   GeneID; 3433565; -.
DR   KEGG; cjk:jk2075; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000545; 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; 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: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; 2.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..976
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334746"
FT   MOTIF           63..74
FT                   /note="'HIGH' region"
FT   MOTIF           745..749
FT                   /note="'KMSKS' region"
FT   BINDING         748
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   976 AA;  108844 MW;  F70D707285B5C31E CRC64;
     MTNGSTEDNS YRYTPGLAAK IEAKWQKHWA DKGTFNAPNP TGDLAEPGAE LPEDRKFIQD
     MFPYPSGVGL HVGHPLGYIG TDVFARFHRM KGANVLHTLG YDAFGLPAEQ YAVQTGTHPR
     TTTMANIANM ERQLGRLGLG HDKRRSFATT DTDYYRWTQW IFLQIYNSWF DPEAKNANGT
     LGKARPIKEL EEKLAAERAD WADLSAAEKQ EILDSYRLVY RSNSTVNWCP GLGTVLANEE
     VTAEGRSERG NFPVFRKNLQ QWMMRITAYS DRLIDDLEYL DWPEKVKSMQ RNWIGRSRGA
     EVTFDCLGND IDVFTTRPDT LFGATYMVLA PEHELVDTLV AQSGNSSSGS DAYTDVDPRW
     TYGQANPAAA VEAYRAAIAA KSDLERQENK EKTGVFLGVY ATNPVNGAQV PVFIADYVLT
     GYGTGAIMAV PAHDSRDFEF ATEFGLPIVP VLAPEGAEAG AGEQGGAELT EAFTEDGPHI
     NSNNSDGLEL NGLGKAEAID KAIEWLESKG VGSGKIQYKL RDWLFARQRY WGEPFPIVYD
     EDGTAHGLPE DMLPVELPEV EDYKPVSFDP DDKDSAPQPP LAKAKDWVEV TLDLGDGEKT
     YYRDTNVMPQ WAGSSWYQLR YIDPNNDNAL VDIENERYWV GPREGRPSGG VDLYVGGVEH
     AVLHLLYARF WHKVLFDLGV VSSFEPYYRL YNQGYIQAYA YTDSRGVYVP AEEVTERDGK
     FFWVRKADDA EGVTKEEEVF QEYGKMGKSL KNAVSPDEIC DDYGADTLRV YEMAMGPLDT
     SRPWATKDVV GAQRFLQRAW RLAVDENTGK GSVSDDALTD EDLKALHRTI AGVHENYAEL
     RDNTAVAKLI EYVNYLTKTY SAGQAPRAAV EPLVQMLSPV APHIAEEMWE ILGHSEGITY
     ESFPEWDEKW LVDDTIELPV QVMGKLRGRI NVAADASRED IEAAALEEPN VASHIEGKTV
     AKIIVVPGKM VNIVAK
//