ID   SYL_BUCAI               Reviewed;         859 AA.
AC   P57519;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=BU444;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13142.1; -; Genomic_DNA.
DR   RefSeq; NP_240256.1; NC_002528.1.
DR   RefSeq; WP_010896120.1; NC_002528.1.
DR   AlphaFoldDB; P57519; -.
DR   SMR; P57519; -.
DR   STRING; 107806.10039108; -.
DR   EnsemblBacteria; BAB13142; BAB13142; BAB13142.
DR   KEGG; buc:BU444; -.
DR   PATRIC; fig|107806.10.peg.454; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001806; 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..859
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151987"
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   859 AA;  102170 MW;  43DBB88CD4020975 CRC64;
     MEKEYSPKKI ENYVQEFWKK NKTFEVKEDP KKEKYYCLPM LPYPSGKLHM GHVRNYTISD
     VISRYQRMLG KNVLQPMGWD AFGLPAEEAA IRNNTDPFSW TQKNIKYMKK QLQSLGFSYD
     WSREITTCHP EYYHWEQWFF TKLYEKKLVY KKNSLVNWCS YDKTVLANEQ VIDGCCWRCQ
     NKIRIKQIPQ WFIKIRNYAE SLYQDLKKLT HWPENVKNMQ RNWIGRIKGF EITLNVFNTC
     QKLKVFTQRL DLLMGVTYIS ISSCHKLSIN LSKKNELIKK FIKKYRYISQ EEQYKVKYTG
     INTNLFVVHP ITKKTIPIWI SNATHIEYGT NAVLSIPGHN ENDWNFAVKN NLKIKYVIFN
     PDHQEPKLYT SFLDIKGTLF NSQEFNGLNL KDGTEKIKKI LYKKKILKEK INYKLQDWCI
     SRQRYWGTPI PMAKFKNGKM IPIPENQLPV VLPKIRKNTN LLQQAINFNS KWAEIFIHGK
     HAIREIDTFD TFMESSWYYA RYTCPNFNTG MIDSIASKYW LPVDQYIGGI EHAIMHLMYF
     RFYHKLLRDF KLVDFDEPVK NLLCQGMVLS EAFYKIDSNS QRKWFNSSSV LIKRNTKGEI
     IESHTQKGEK LIYAGMIKMS KSKNNGIEPE LIIQRYGADT IRLFIMFSAP VESDLEWKES
     GLKGIYRFLK KLWMLIFNYI DIKNTHKKIN FDFLNHQQSE LRYQLHKTIA KVSDDIGRRQ
     TFNTAISEIM KLVNQLSKAP IKEEQDKSIM RESLICIIKM LYPFTPHFCF FVWNYFNNHS
     SIDNEKWPIF QKDILSKKYS TIVAQINGKK RCATKISDSL TKEEIFLYIQ NQPIIKKYLE
     DVDIKKIIYI PKKIINFVT