ID   SYL_CLAM3               Reviewed;         851 AA.
AC   A5CR89;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=CMM_1547;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382;
RX   PubMed=18192381; DOI=10.1128/jb.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA   Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM711867; CAN01594.1; -; Genomic_DNA.
DR   RefSeq; WP_012038234.1; NC_009480.1.
DR   AlphaFoldDB; A5CR89; -.
DR   SMR; A5CR89; -.
DR   KEGG; cmi:CMM_1547; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001564; 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   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; 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; 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; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..851
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334743"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           615..619
FT                   /note="'KMSKS' region"
FT   BINDING         618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   851 AA;  94950 MW;  42B1FC0B7736F1B6 CRC64;
     MAHETPDTPG ETYDFRAIEA EWSEVWEREQ PFRTPDASDS RPRKYILDMF PYPSGDLHMG
     HAEAFALGDA VARYWRQQGF NVLHPIGWDS FGLPAENAAI KRGVDPREWT YANIETQKQS
     MKRYGLSFDW ERELHTSDPE YYRWNQWLFL KMHEKGLAYR KDSWVNWDPV DQTVLANEQV
     LPDGTSDRSG AVVVKKKLTQ WYLRITDYAD RLVDDLNQLE GTWPAKVISM QRNWIGRSIG
     AEVDFVVEGR DEPVTVFTTR PDTLHGATFM VVAPDSDLAA ELVEGASDEV RERFRGYLER
     TQRLNEIERS TTDRPKTGIP LGRTAINPVN GERIPVWAAD YLLADYGTGA VMAVPAHDQR
     DLDFARAFDL PVRVVVDTTQ PVTGAIRIIP EDGELPDLEE VLPGRTGVAL PGEGRLINSG
     SLNGLSKQPA IKRVIEQLEA EGRGRAAKNY RLRDWLISRQ RFWGTPIPIV YDAEGNEIRV
     PEDQLPVRLP DTEGLDLAPK GKSPLAAATE WTNVPSPVDG SPATRDPDTM DTFMDSSWYW
     LRFLSPNDAT KAFDPADADR WAPIDQYVGG VEHAILHLLY SRFITKVLFD LGYVTFTEPF
     SALLNQGMVL SGGSKMSKSK GGVDLGSEMD RHGVDAIRLT MAFAGPPEDD IDWEDVSPSG
     SAKFLARAWR LTGDITSAPE IEWKTGDEAL RRVTHRFLAE APGMLEAFKF NVVIARTMEL
     VNAIRKTIDQ GPGGGDAAVR EATEVVAIAL SLFAPYTAED MWRRLGREGS VAFAGWRKAE
     RNLLVQSTVT AVVQVDGKVR DKLEVDAKIG ADELEALARE TAGVKRSTAG RTIDKVIVRA
     PKIVSITTTA P
//