ID   SYL_HAMD5               Reviewed;         869 AA.
AC   C4K7R7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=HDEF_2038;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(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; CP001277; ACQ68610.1; -; Genomic_DNA.
DR   RefSeq; WP_015874363.1; NC_012751.1.
DR   AlphaFoldDB; C4K7R7; -.
DR   SMR; C4K7R7; -.
DR   STRING; 572265.HDEF_2038; -.
DR   EnsemblBacteria; ACQ68610; ACQ68610; HDEF_2038.
DR   GeneID; 66261587; -.
DR   KEGG; hde:HDEF_2038; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000002334; 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   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; 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..869
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000202222"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           620..624
FT                   /note="'KMSKS' region"
FT   BINDING         623
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   869 AA;  100422 MW;  0A84DC84D4B2F361 CRC64;
     MQDIYRHQDI ESHVQRHWEQ TQTFTVKEDP KKEKYYCLAM WPYPSGRLHM GHVRNYTITD
     VIARYQRMLG KNVLQPMGWD AFGLPAEGAA IKNKTSPIDW TKANIQYMKK QLQSLGFAYD
     WSRELTSCKP EYYRWEQWFF TQLYEKGLVY KKTSDVNWCP QDFTVLANEQ VIDGRCWRCD
     SKVERKSIPQ WFIKITAYAD QLLDDLDELE HWPEQVKTMQ RHWIGRSEGV EIRFPLDHDE
     KTDLTVYSTR PDTLMGVAFI AIAPDHFFSA EIAKNVPALA TFIEECRHIK MAEAETATIE
     KKGIDTGFFA LHPLTGKKIP IWVANFVLME YGTGAVMGVP GHDQRDWEFA TQYHLPIKAV
     ILLEDGTEPD VQKKPLIEKG RLCHSGEFNG LSYQESCDRI IDKLVDLGTG QRKVNYRLRD
     WGVSRQRYWG APIPMITLED GRIIGTPEDQ LPVILPEKTL IKDMINPLKA DQDWAKTSVA
     GQLGIRETDT FDTFIESSWY YARYACPKYD QGMIEKAAAN YWLPVDQYVG GIEHAIMHLL
     YFRFFHKLMR DQGLVDSKEP AKRLLCQGMV LADAFYYNAQ NGERVWVSPT EVTVERDNKG
     QFLNAFDAQG RDLIHAGMSK MSKSKNNGID PQAIVEKYGA DTVRLFMMFA SAPEMTLEWQ
     ESGLEGAYRF LKRLWRFVFD HVIQGPTQPL KKENLNSTQK NLRRNLHKTI AKVTDDIGRR
     QTFNTAIAAI MELMNQLYRA PTNTEQDRAL IQEACISVIK MLYPFTPHIS FILWQHLHQS
     PDETHPLNID DSLWPVVDQN ALIEDETLVV IQINGKMRAK ITVPMNSTQQ EVYESALQEP
     TVIKHLKGIT PCHVIYVPNK LLNLVVNNE