ID   SYL_LACAC               Reviewed;         804 AA.
AC   Q5FIP3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=LBA1617;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV43431.1; -; Genomic_DNA.
DR   RefSeq; WP_003548508.1; NC_006814.3.
DR   RefSeq; YP_194462.1; NC_006814.3.
DR   AlphaFoldDB; Q5FIP3; -.
DR   SMR; Q5FIP3; -.
DR   STRING; 272621.LBA1617; -.
DR   GeneID; 56943182; -.
DR   KEGG; lac:LBA1617; -.
DR   PATRIC; fig|272621.13.peg.1537; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   BioCyc; LACI272621:G1G49-1579-MONOMER; -.
DR   Proteomes; UP000006381; 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; Reference proteome.
FT   CHAIN           1..804
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091324"
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;  92469 MW;  0140B1FBDD5040B2 CRC64;
     MYNHKVVEKK WQDYWAKHDT FKTGTDSNKK NYYALDMFPF PSGKGLHVGH PEGYTATDIV
     SRMKRAQGYN VLHPMGWDAF GLPTEQYALK TGEDPEVVTK NNIANFKRQL NKLGFSYDWD
     REVTTSDPNY YKWTQWVFEQ MYKKGLAYEA EVPVNWSPDL GTVVANEEIV DGKTERGGYP
     VYRRNMRQWM LKMTAYADRL LEDLDDLDWP EPVKEMQRNW IGRSLGAQVT FKIKDSDKTF
     DIFTTRPDTL FGCSYTVLAP ENKLVQEITT DAQRDEVNAY IKKIESKSDL ERTDLNKDKT
     GVFTGAYAIN PVNGKEVPIW ISDYVLASYG TGAVMAVPAH DERDYAFATK FGLPINPVLE
     GGDITKEAFT EDGPHINSEF LNGLNIKDAK KKMVEWLEEH NCGEKKVNYK LRDWDFSRQR
     YWGEPIPVIH WEDGETTLVP EDQLPLRLPH ATDIKPSGTP ESPLANLTDW VNVVDENGRK
     GKRETNTMPN WAGSSWYYLR YVDPHNDKEL ADYDLLKKWL PVDLYIGGAE HAVRHLLYAR
     FWHKVLYDLG VVPTKEPFQR LYNQGLILKN HEKMSKSKGN VVNPDDVIDE YGADSLRMYE
     MFMGPLDASI DWDDNGPAST KKFLDRVWRL FVNDLDLKAI PQERIVDEND GELDKVYAET
     VKKVTEDFDA LHFNTAISQM MVFMNAAQKA KTIPREYAEG FVKLLAPVAP HMMEEIWQVF
     GHDESISYAE WSTYDPAKLV ESTVEIMVQV NGKLRGKFQA AKDADRDEVQ KQAMELPHVQ
     KFLEGKDVKK VIVVPNKIVN IVAK
//