ID   SYL_BUCBP               Reviewed;         861 AA.
AC   P59433;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=bbp_395;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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; AE016826; AAO27107.1; -; Genomic_DNA.
DR   RefSeq; WP_011091508.1; NC_004545.1.
DR   AlphaFoldDB; P59433; -.
DR   SMR; P59433; -.
DR   STRING; 224915.bbp_395; -.
DR   PRIDE; P59433; -.
DR   EnsemblBacteria; AAO27107; AAO27107; bbp_395.
DR   GeneID; 56470932; -.
DR   KEGG; bab:bbp_395; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000601; 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; -; 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; 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; PF00133; tRNA-synt_1; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151989"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           618..622
FT                   /note="'KMSKS' region"
FT   BINDING         621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   861 AA;  101600 MW;  35F7B75BE5A45012 CRC64;
     MKQNYCPKTI EPYVQSIWKK KNTFKVTENS NKEKFYCLAM IPYPSGKLHM GHVRNYTISD
     VIARYQRMLG KNVLHPMGWD AFGLPAENAA IKNNTHPAQW TYENIKYMKQ QLISLGLSYD
     WDREITTCKP EYYQWEQWFF IELYKKNLVY KKKSWVNWCE YDKTVLANEQ VINELCWRCN
     NKVIKKKIFQ WFIKITKYAE ELLNDLDNLP EWPEKVKTMQ HNWIGRNHGI KIKLKLANQH
     TILNDVFISK PSTLMGATFI TLSPSHELSF KIARKKHKIQ EFIENCSSNT NTYNDINNTN
     IGINTNEFAL HPITKKKLPI WITNYVLSDY DTNSILCVPA HNQHDLNFAI KYNLKIKAVI
     LNLDGTEPKI KNTAMTSMGK LFNSNQYNNL NYQEGSYRII QDLENNHIGK KITYYRLRDW
     SISRQRYWGA PIPMAVLENK KNVPIPKQYL PIILPETIPF KNIKPLSNNI LLKKIYIDEK
     IAICESDTFD TFLESSWYYA RFTCNNFHKG MISQKLANYW LPVDQYIGGI EHAVMHLIYF
     RFVHKLLRDL GLVYSNEPVK KLLCQGMVLS DAFYYFDHNK QKQWISAKSI TIKYDSNHKI
     QSHFYSNNKK IFHAGMIKMS KSKFNGIEPE DIIKKYGTDT IRLFIMFAAP VESALEWKES
     GVKGIHKFLK KLWVLSYNHI KLYNHKIKLR INLFTEQQQH IYSELHKTIK IVSQYITDTQ
     SFNVAISKIM KFSNTLMSIS LKNEQNQALM QESLLAVIQM LYPFIPHFSF AIWEFLSPKK
     ENIDFISWPK YNFKAILSKL KYTIIIQING KKRHKILALK NSSQEKILEI ILNENKIKKY
     LNNKPIQKII YIPNKILNLV I