ID   SYL_BACTN               Reviewed;         944 AA.
AC   Q8A329;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, 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};
GN   OrderedLocusNames=BT_3126;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO78232.1; -; Genomic_DNA.
DR   RefSeq; NP_812038.1; NC_004663.1.
DR   RefSeq; WP_011108648.1; NC_004663.1.
DR   AlphaFoldDB; Q8A329; -.
DR   SMR; Q8A329; -.
DR   STRING; 226186.BT_3126; -.
DR   PaxDb; 226186-BT_3126; -.
DR   EnsemblBacteria; AAO78232; AAO78232; BT_3126.
DR   GeneID; 60924307; -.
DR   KEGG; bth:BT_3126; -.
DR   PATRIC; fig|226186.12.peg.3189; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   InParanoid; Q8A329; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   Gene3D; 3.40.50.620; HUPs; 3.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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..944
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151974"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           718..722
FT                   /note="'KMSKS' region"
FT   BINDING         721
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   944 AA;  108569 MW;  551BEBFCD0F19DA1 CRC64;
     MEYNFREIEK KWQQRWVEEK TYQVTEDESK QKFYVLNMFP YPSGAGLHVG HPLGYIASDI
     YARYKRLRGF NVLNPMGYDA YGLPAEQYAI QTGQHPAITT KANIDRYREQ LDKIGFSFDW
     SREIRTCEPE YYHWTQWAFQ KMFNSYYCND EQQARPIQEL IDAFAIYGNE GLNAACSEEL
     SFTAKEWKAK SEKEQQEILM NYRIAYLGET MVNWCQALGT VLANDEVIDG VSERGGFPVV
     QKKMRQWCLR VSAYAQRLLD GLDTIDWTES LKETQKNWIG RSEGAEVQFK VKDSDLEFTI
     FTTRADTMFG VTFMVLAPES DLVAQLTTPA QKAEVDAYLD RTKKRTERER IADRSVTGVF
     SGSYAINPFT GEAVPIWISD YVLAGYGTGA IMAVPAHDSR DYAFAKHFGL EIRPLVEGCD
     VSEESFDAKE GIVCNSPRPD VTPYCDLSLN GLTIKEAIEK TKQYVKEHNL GRVKVNYRLR
     DAIFSRQRYW GEPFPVYYKD GMPYMIDEDC LPLELPEVDK FLPTETGEPP LGHAKEWAWD
     TVNKCTVENE KIDNVTIFPL ELNTMPGFAG SSAYYLRYMD PHNNKALVDP KVDEYWKNVD
     LYVGGTEHAT GHLIYSRFWN KFLHDVGASV VEEPFQKLVN QGMIQGRSNF VYRIKDTHTF
     VSLNLKDQYE VTPLHVDVNI VSNDILDLEA FKAWRPEYAE AEFILEDGKY ICGWAVEKMS
     KSMFNVVNPD MIVDKYGADT LRMYEMFLGP VEQSKPWDTN GIDGVHRFIR KFWSLFYSRT
     DEYLVKDEPA TKEELKSLHK LIKKVTGDIE QFSYNTSVSA FMICVNELSN LKCNKKEILE
     QLVITLAPFA PHVCEELWDT LGHETSVCDA AWPAYNEEYL KEDTINYTIS FNGKARFNME
     FDADAASDAI QAAVLADERS QKWIEGKTPK KIIVVPKKIV NVVV
//