SYL_LACPL
ID SYL_LACPL Reviewed; 808 AA.
AC Q88XA9; F9UN89;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=lp_1316;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC78678.1; -; Genomic_DNA.
DR RefSeq; WP_003643180.1; NC_004567.2.
DR RefSeq; YP_004889192.1; NC_004567.2.
DR AlphaFoldDB; Q88XA9; -.
DR SMR; Q88XA9; -.
DR STRING; 220668.lp_1316; -.
DR EnsemblBacteria; CCC78678; CCC78678; lp_1316.
DR GeneID; 66449185; -.
DR KEGG; lpl:lp_1316; -.
DR PATRIC; fig|220668.9.peg.1110; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR PhylomeDB; Q88XA9; -.
DR BioCyc; LPLA220668:G1GW0-1136-MON; -.
DR Proteomes; UP000000432; 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; 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 PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 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..808
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152030"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 580..584
FT /note="'KMSKS' region"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 808 AA; 92629 MW; 68FE11F39F61821F CRC64;
MAYNHKVIER KWQHYWKENK TFKTLDTTDK KKYYALDMFP YPSGQGLHVG HPEGYTATDI
MSRFKRMQGY NVLHPMGWDA FGLPAEQYAL KTGHNPKDFT AKNIKNFKRQ IRSLGFSYDW
DREVNTTDPS YYKWTQWIFE QLYKKGLAYE SETLVNWAPD MMGGTVVSNE EVVDGKTERG
GYDVYRVPMK QWSLKITAYA DRLIDDLDDI DWPENIKEQQ RNWIGRSVGA SIRFKVAGQP
DDTEIEVFST RPDTLFGASY MVLAPEHDLV EQLTTPEQAD AIKAYKAKIA SKSDLERTDL
NKDKTGVFTG SYGINPVNGE KLPIWIADYV LASYGTGAIM AVPAHDDRDF EFAQKFDLPI
KPVIAGDNDY DQQAYTGDGE HINSGFVDGL AKQPAIDKMI DWLGEHHAGE KKVNYRLRDW
IFSRQRYWGE PIPVIHWEDG ETTLVPEDEL PLRLPATKNL EPSGTGESPL ANIDDWVNVV
DENGRKGKRE TNTMPQWAGS SWYFLRYVDP HNREALADYD KLKYWSPVDL YVGGAEHAVL
HLLYARFWHK FLYDLGVVPT KEPFQKLVNQ GMILGDNHEK MSKSRGNVVN PDDIVDQYGA
DTLRLYEMFM GPLEASIPWS TDGLHGANKW IERVWRLMID ENNRVRDRIT TINDGKLTKI
YNETVKKVTE DYEAMRFNIA ISQMMVFVNE AYKVDDLPII YIEGFVKLLS PIAPHLSEEL
WSLLGHDDTI TYATWPTYDE SKLVEDTVQI VLQVNGKVRS HAEVAKDMGK DELEKLALAD
EKIQEFTAGK TVRKVIAIPG KLVNVVAN
