ID   SYL_BIFAA               Reviewed;         990 AA.
AC   A1A1R2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 101.
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}; OrderedLocusNames=BAD_0864;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009256; BAF39645.1; -; Genomic_DNA.
DR   RefSeq; WP_011743229.1; NC_008618.1.
DR   AlphaFoldDB; A1A1R2; -.
DR   SMR; A1A1R2; -.
DR   STRING; 1680.BADO_0919; -.
DR   EnsemblBacteria; BAF39645; BAF39645; BAD_0864.
DR   KEGG; bad:BAD_0864; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000008702; 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   Gene3D; 3.40.50.620; -; 3.
DR   Gene3D; 3.90.740.10; -; 1.
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   PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..990
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334732"
FT   REGION          573..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           74..85
FT                   /note="'HIGH' region"
FT   MOTIF           763..767
FT                   /note="'KMSKS' region"
FT   COMPBIAS        585..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         766
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   990 AA;  110940 MW;  D87EB57E09014058 CRC64;
     MSDTEKSAQA QPNESAEPSF RYNAKLAQGI EEKWQKIWDD EGTFWAANVN GDLKDGKGHN
     AEGRPSYFAM DMFPYPSGKG LHVGHPLGYL ATDVVSRYHR MKGENVLHAM GYDAFGLPAE
     QYAVQTGQHP RITTEQNIAN MRRQLHRMGL SFDNRRSFAT IDPGYVRWTQ WIFSRIYDAW
     YDEDATNPSG SRGCARPIST LVEQFESGKR AIPGFEGKAW ADLSEAEQAD VLNDFRLAYI
     SKSPVNWCPG LGTVLANEEV TAEGKSERGN FPVFQRELRQ WSMRITAYGH RLIEDLDTID
     WPEKVKLMQR NWIGESHGAS VHFDVETPNG VKDMEIYTTR PDTLFGTTFA VVSPEHHLLE
     DVPAEWPAET PEDWKGGYAT PVEAVKAYRL AAEAKTAKDR VDEAGEKTGL FTGLYAINPI
     TGAKLPLFTA DYVLMDYGTG AIMAVPGGDQ RDYDFAVKFG LPVIYTVKPL PESGDDLANY
     EGKAPFVSHD GIVINSSIDA TKAKGDSLSL DGLRVDEAID KVNAWLESAG VGKGTVSYRL
     RDWLFSRQRY WGEPFPIVYG EDGTPHLLPD EQLPINLPDV PDYSPKTFDP EDAESDPEAP
     LSRNEDWVKV ELDLGDGKKT YYRDTNTMPN WAGSCWYYMR YLDPTDTKHM VEKDEFDYWM
     GPDHNKTAGK SGGVDLYIGG VEHAVLHLLY SRFWHKVLFD LGYVDSMEPF HKLFNQGMIQ
     AYAYTDDRGQ YVPAAEVVEG PADANGEPTF TWNGQHANRE FGKMGKSLKN IITPDDMYEN
     YGADTFRLYE MGMGPLAESR PWNTRNVVGS MRFLQRLWRN VIDETTGEVR VTDGELDTKT
     LKLLNNTIAD VTVEMEAMRP NTAIAKLIVL NNHLTSLDAV PRAAVEPLIL MLSPIAPHIC
     EELWSKLGHT ESLAHADWPK ADERYVGQDS VTAVVQIKGK VRAKLEVSPD IDPKELEKMA
     LEAVADRLGG KEPRKVIVKA PKIVSIVPAE