ID SYL_LACLA Reviewed; 829 AA.
AC Q9CHB6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, 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=LL0816;
GN ORFNames=L0352;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AE005176; AAK04914.1; -; Genomic_DNA.
DR PIR; H86726; H86726.
DR RefSeq; NP_266972.1; NC_002662.1.
DR RefSeq; WP_003132571.1; NC_002662.1.
DR AlphaFoldDB; Q9CHB6; -.
DR SMR; Q9CHB6; -.
DR PaxDb; 272623-L0352; -.
DR EnsemblBacteria; AAK04914; AAK04914; L0352.
DR KEGG; lla:L0352; -.
DR PATRIC; fig|272623.7.peg.872; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000002196; 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; 3.40.50.620; 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; 2.
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..829
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152029"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 609..613
FT /note="'KMSKS' region"
FT BINDING 612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 829 AA; 93791 MW; F0F0A43014F6C389 CRC64;
MEYNHQEIEA KWQKYWADNK TFRTGTDKNK PKFYALDMFP YPSGAGLHVG HPEGYTATDI
LSRYKRAQGF NVLHPMGWDA FGLPAEQYAM DTGNDPAEFT AENIANFKRQ INSLGFSYDW
EREVNTTDPN FYKWTQWIFT KLYEKGLAYE AEVAVNWVEE LGTAIANEEV LPDGTSERGG
YPVVRKPMRQ WMLKITAYAE RLLEDLEEVD WPESIKEMQR NWIGKSVGAD VTFEVAGTDK
SFEVFTTRPD TLFGATYAVL APEHDLVDAI TTPEQKEAVA EYRRKASLKS DLARTDLSKE
KTGAFTGAYA INPINGRKMP IWVADYVLAS YGHGAVMAVP AHDERDWEFA KVYGLEILPV
VEGGNVEEAV YTEDGPHINS EFLNGLDKAQ AIEKAIEFLE EKKIGKKKIT YRLRDWLFSR
QRYWGEPIPI IHWEDGTSTA LSEDELPLVL PVTSDIKPSG TGESPLANLT DWLEVTRADG
LKGRRETNTM PQWAGSSWYY LRYIDPNNSE ALADPELLKE WLPVDIYVGG AEHAVLHLLY
ARFWHKVLYD LGVVPTKEPF QKLFNQGMIL GTSYRDHRGA LVATDKVEKR DGGFYHMETG
EALEQAPAKM SKSLKNVVNP DDVVEHYGAD TLRVYEMFMG PLDASIPWSE EGLEGARKFL
DRAVRMIENS EIKAENNGEL DKVYNETVKN VTERLDLMYF NTAISQLMIF VNAVNKAKAL
PLEYANGFVQ LLAPFAPHIA EELWVKLGNE AGISYVAWPT FDESKLIESE VEIVVQINGK
LKAKIKIAKD LAREELEKIG RESVAEALEG KNVVKVIAVP NKLVNIVVK
//
