ID   SYL_BUCCC               Reviewed;         847 AA.
AC   Q057G3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=BCc_274;
OS   Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=372461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cc;
RX   PubMed=17038625; DOI=10.1126/science.1130441;
RA   Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA   Silva F.J., Moya A., Latorre A.;
RT   "A small microbial genome: the end of a long symbiotic relationship?";
RL   Science 314:312-313(2006).
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; CP000263; ABJ90736.1; -; Genomic_DNA.
DR   RefSeq; WP_011672655.1; NC_008513.1.
DR   AlphaFoldDB; Q057G3; -.
DR   SMR; Q057G3; -.
DR   STRING; 372461.BCc_274; -.
DR   KEGG; bcc:BCc_274; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000669; 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; 2.20.28.290; -; 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; 2.
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..847
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334735"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           607..611
FT                   /note="'KMSKS' region"
FT   BINDING         610
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   847 AA;  101253 MW;  A1330936B233079C CRC64;
     MKNNNYNPKK IEKYVQKYWV KKKIFFTKID KEKKKFYCLP MLPYPSGKLH MGHVRNYTIS
     DVISRFHRML GKNVLQPIGW DSFGLPAEET AIKNNISPKK WTFKNIKTMK KQLQSLGFSY
     DWNKEITTCN PEYYRWEQLF FIKLFKKKLI YKKKSIVNWC EKDKTVLANE QVQKGVCWRC
     GTKIKLRKIS QWFIKIKKYA DKFLKDLKLL KKWPKEVISM QKNWIGKSKG LKIKCKIYKK
     KYFLKIFTTK PETIMGISFF AISMYHPLIN LFLRKNIEIQ KFLKKNKYSI NTEFQKSNIL
     FGINTHLYVI HPINKKKIPL WISNYVKYNY ATGAIMSVPC SNKIDYNFSK LYNIPFIKIF
     SKKNKKLLIN SDNFNNLNIK KARNKISNFL INKKIAKKYI YYKIQDWCIS RQRYWGTPIP
     IVIDNKKNII TVPKKKLPVI LPKYIYKKKS LQSLSLYSLW LKTKISGKKV TRETDTLDTF
     MESSWYYARY TNPKYEKDII DPKASEYWLP VDQYIGGIEH AVMHLIYFRF YHKLLYDFGY
     VQSKEPVKKL ICQGMVIIDS FYKYNKDGSK KWLSISKIEI NRDSKGKIIS AIEKSSQKKI
     IYAGKIKMSK SKNNGIDPVN IIKQYGADSL RLFIMFAAPI NISLEWNSKN IIGMHRFLKK
     IWNFVFIIIK KKKEKIKKID LNKNKKTYIY KLNTIIKKVT YNIQERNSFN TAIAEIIKFF
     NYLVKLYKIY NIKKKNLIFC ISTIIKMLYP FTPHICFILW KKIYGKKSCI EKETWPKFNK
     KFFLKEKNNI IIQINGKKKD IMKIHAIISK KEIIKLILKN EKIKKHLYKK IIKKTIYIPN
     KVINFVL
//