ID   SYL_LACJO               Reviewed;         804 AA.
AC   Q74KS1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 139.
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=LJ_0680;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS08498.1; -; Genomic_DNA.
DR   RefSeq; WP_011161628.1; NC_005362.1.
DR   AlphaFoldDB; Q74KS1; -.
DR   SMR; Q74KS1; -.
DR   KEGG; ljo:LJ_0680; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   Proteomes; UP000000581; 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   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; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..804
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091329"
FT   MOTIF           39..50
FT                   /note="'HIGH' region"
FT   MOTIF           573..577
FT                   /note="'KMSKS' region"
FT   BINDING         576
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   804 AA;  92336 MW;  8D7EAB45725646A9 CRC64;
     MYNHKTVEKK WQKYWAEHDT FKTGTDPKKK NYYALDMFPF PSGKGLHVGH PEGYTATDIV
     SRMKRAQGYN VLHPMGWDAF GLPTEQYALK TGEDPEKVTK ENIANFKKQL NKLGFSYDWD
     REVTTSDPNY YKWTQWVFEQ MYKKGLAYEA EVPVNWSPDL GTVVANEEII DGKTERGGYP
     VYRRNMRQWM LKMTAYADRL LEDLDDLDWP EPVKEMQRNW IGRSEGAQVT FKVKDSDKTF
     DVFTTRPDTL FGVSYTVLAP ESKLVQEITT PEQKEAVDAY IKKIESKSDL ERTDLNKDKT
     GVFTGAYAVN PVNGKEVPIW ISDYVLASYG TGAVMAVPAH DDRDYAFATK FGLPINRVIE
     GGNLEKEAFG GDGKHINSEF LDGLNNEEAK KRMIEWLEDH NVGEKKVNYK LRDWDFSRQR
     YWGEPIPVIH WEDGTTSLVP EDELPLRLPH ATDIKPSGTP ESPLANLTDW VNVVDENGRK
     GKRETNTMPN WAGSSWYYLR YIDPHNDKEL ADYDLLKKWL PVDLYIGGAE HAVRHLLYAR
     FWHKVLYDLG VVPTKEPFQK LYNQGLILKN HEKMSKSKGN VVNPDEVIDE YGADSLRMYE
     MFMGPLDASI DWDDNGPAST KKFLDRVWRL FVNDLDLKAI PQEKIVDEND GELDKVYAET
     VKKVTEDFEA LHFNTAISQM MVFMNAAQKA KTIPREYAEG FVQLLAPVAP HMMEEIWSVF
     GHDESIAYAK WPEYDPAKLV ESTVEIMVQV NGKLRGKFKA AKDSDKDTLE KEALALDHVQ
     KFLEGKDVKK VIVIPNKIVN IVAK
//