ID F7QUW9_9LACO Unreviewed; 805 AA.
AC F7QUW9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN ORFNames=LSGJ_01507 {ECO:0000313|EMBL:EGM50959.1};
OS Ligilactobacillus salivarius GJ-24.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1041521 {ECO:0000313|EMBL:EGM50959.1, ECO:0000313|Proteomes:UP000003074};
RN [1] {ECO:0000313|EMBL:EGM50959.1, ECO:0000313|Proteomes:UP000003074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GJ-24 {ECO:0000313|EMBL:EGM50959.1,
RC ECO:0000313|Proteomes:UP000003074};
RX PubMed=21742893; DOI=10.1128/JB.05616-11;
RA Cho Y.J., Choi J.K., Kim J.H., Lim Y.S., Ham J.S., Kang D.K., Chun J.,
RA Paik H.D., Kim G.B.;
RT "Genome Sequence of Lactobacillus salivarius GJ-24, a Probiotic Strain
RT Isolated from Healthy Adult Intestine.";
RL J. Bacteriol. 193:5021-5022(2011).
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:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363035}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGM50959.1}.
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DR EMBL; AFOI01000004; EGM50959.1; -; Genomic_DNA.
DR RefSeq; WP_003708263.1; NZ_AFOI01000004.1.
DR AlphaFoldDB; F7QUW9; -.
DR PATRIC; fig|1041521.3.peg.1516; -.
DR Proteomes; UP000003074; Unassembled WGS sequence.
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 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; 1.
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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 39..170
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..400
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 413..603
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 655..765
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 576..580
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 805 AA; 92243 MW; 3E5833B7C48EDA04 CRC64;
MSYKHIEIEK KWQRYWEEHK TFKTTEDDDK KNYYALDMFP YPSGQGLHVG HPEGYTATDI
MARMKRMQGY NVLHPMGWDA FGLPAEQYAL NTGNSPREFT KKNINNFRRQ IKSLGLSYDW
DREVNTTDPA YYKWTQWIFE QLYKKGLAYE AEVPVNWSPD LGTVVANEEV IDGKTERGGF
PVIRKPMRQW VLKITAYADR LIDDLDDLDW PEAIKEQQRN WIGRSVGAAI NFPVSGDENT
KIEVFSTRPD TIFGVAALVL APEHELVKQL TTPEHENEVE AYIEKISHKS DLERTDLAKD
KTGVFTGSYV VNPVSGEKLP IWIADYVLNS YGTGAVMVVP AHDERDHEFA QKFDLPIVQV
IEGGDVQKEA YTGDGVHINS DFLNGMDKDE AIDAINNWLE ENGVGEKKVN YRLRDWLFSR
QRYWGEPIPV IHWEDGETTL VPEDELPLYL PKATDIKPSG TGESPLANLD DWVNVVDENG
RKGRRETNTM PQWAGSSWYF LRYIDPHNNH EVADYEKLKE WLPVNLYVGG AEHAVLHLLY
ARFWHKFLYD LGVVPTKEPF QKLVNQGMIL GSNHEKMSKS KGNVVNPDDI VEQYGADTLR
LYEMFMGPLD ASIPWSEEGL GGAHKFINRV WNLLIDENDN LRDRVTTINN HELDKIYNET
VKKVTEDYEA MHFNTAISQL MVFVNNAYKA DSLPLEYVEG LVKLLSPVVP HITEELWSKL
GHVGSIAYAK WPTYDESKLV EDVVEIVVQI NGKVRQHLQV SKDASREELQ ALALNDERIK
QELVDKEVKK VIAVPGKLVS IVVAK
//
