ID SYL_CLAMS Reviewed; 852 AA.
AC B0RDA6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-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}; OrderedLocusNames=CMS1760;
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=31964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX PubMed=18192393; DOI=10.1128/jb.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(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; AM849034; CAQ01862.1; -; Genomic_DNA.
DR RefSeq; WP_012299105.1; NZ_MZMN01000003.1.
DR AlphaFoldDB; B0RDA6; -.
DR SMR; B0RDA6; -.
DR STRING; 31964.CMS1760; -.
DR KEGG; cms:CMS1760; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000001318; 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..852
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334744"
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 852 AA; 94838 MW; 3FFE4D7CEC276D8D CRC64;
MAHETPDTPG ETYDFRAIEA EWSEVWEREQ PFRTPDASDS RPRKYILDMF PYPSGDLHMG
HAEAFALGDA VARYWRQQGF NVLHPIGWDS FGLPAENAAI KRGVDPREWT YANIETQKQS
MKRYGLSFDW ERELHTSDPE YYRWNQWLFL KMHEKGLAYR KDSWVNWDPV DQTVLANEQV
LPDGTSDRSG AVVVKKKLTQ WYLRITDYAD RLVDDLNQLE GTWPAKVLSM QRNWIGRSIG
AEVDFVVEGR DEPVTVFTTR PDTLHGATFM VVAPDSDLAA ELVEGASEEV RESFRGYLER
TQRLNEIERS TTDRPKTGIP LGLTAINPVN GERIPVWAAD YVLADYGTGA VMAVPAHDQR
DLDFARAFDL PVRVVVDTTQ PVTGAIRIIP EDGELPDLEE VLPGRTGVAL PGEGRLINSG
SLNGLSKQPA IKRVIEQLEA EGRGRAAKNY RLRDWLISRQ RFWGTPIPIV YDAEGSEIRV
PEDQLPVRLP DTEGLDLTPK GKSPLAAATA WSNVPSPVDG SPATRDPDTM DTFMDSSWYW
LRFLSPNDAT KAFDPADADR WAPIDQYVGG VEHAILHLLY SRFITKVLFD LGYVTFTEPF
SALLNQGMVL SGGSKMSKSK GGVDLGSEMD RHGVDAIRLT MAFAGPPEDD IDWEDVSPSG
SAKFLARAWR LTGDITSAPE VEWKTGDEAL RRVTHRFLAE APGMLEAFKF NVVIARTMEL
VNAIRKTIDQ GPGGGDAAVR EATEVVAVAL SLFAPYTAED MWKRLGREGS VAFAGWRKAD
RNLLVQTTVT AVVQVDGKVR DKLEVDAKIG ADELEALARE TAGVRRSTAG RTIDKVIVRA
PKIVSITTTP AP
//
