ID   SYL_ELUMP               Reviewed;         835 AA.
AC   B2KB05;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
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=Emin_0201;
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191;
RX   PubMed=19270133; DOI=10.1128/aem.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(2009).
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; CP001055; ACC97764.1; -; Genomic_DNA.
DR   RefSeq; WP_012414379.1; NC_010644.1.
DR   AlphaFoldDB; B2KB05; -.
DR   SMR; B2KB05; -.
DR   STRING; 445932.Emin_0201; -.
DR   KEGG; emi:Emin_0201; -.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001029; 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; 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..835
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091316"
FT   MOTIF           41..52
FT                   /note="'HIGH' region"
FT   MOTIF           611..615
FT                   /note="'KMSKS' region"
FT   BINDING         614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   835 AA;  95166 MW;  955DAACAC38CCF7C CRC64;
     MTEINFQEID KKQQKIWEDN NLFVTPRLPI NPKFYCLDMF PYPSGQGLHV GHPEGYTASD
     ILVRYKKMKG FDVIHPMGWD AFGLPAENYA IATGVHPAIT TKNNIDNFRR QIKSLGMAYD
     WTREIDTTDP NYYRWTQWIF LQIFKKGLAY ESTVPINWCP SCKTGLANEE VFNGNCERCG
     TKIESKNIRQ WVLKITEYAD RLLEDLEGLD WPESTLAMQR NWIGKSIGAE VDFEIDGHKE
     NLKVFTTRPD TLFGATYMVV SPEHPILEQI TMPEQKAAVK SYQEEAAAKT DFERGDVNKK
     TGVFTGAYAI NPVNGKKIQI WTSDYVLMGY GTGAIMAVPA HDERDYEFAK KFGLEIIEVI
     KSDKGVEKEA FTGDGELVNS DFLNGMKVEQ SKAAMIKFLE EKGVGGAKTT YRLRDWVFSR
     QRYWGEPIPI VHCPKCGVVP VPESELPVKL PEVTNYEPTG TGESPLANVP EWVNTVCPVC
     AGPAKRETNT MPQWAGSCWY YLRYLDPKND KTFVNPEIER ECDPVDCYIG GAEHAVLHLL
     YSRFWHKVLY DLGYVKYKEP YAKLRHQGMI LAYSYRGEDG VYHGYDEVDL SDLQNPKLKT
     TGEKLNSMVE KMSKSKKNVI NPDDILHKYG ADAFRMYEMF MGPFEASKPW DMKGIEGVNR
     FLKRVYAWGE SVETDEVFLS TKELDILRSK TIVKVSEDIE KFNFNTAVSA LMIYFNDLSK
     IKGVPLKHFK TFLALLHPFA PHITEELWSR RKCGPFLVKT AWPEADIMLL RSEDMGLGIQ
     VNGKVRGSIT VNASASDDEI KAKAFEEPNV KKHMEGKALV KVIIVPKRMV NIVVK
//