ID   SYL_BLOPB               Reviewed;         872 AA.
AC   Q492Z3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=BPEN_321;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40951.1; -; Genomic_DNA.
DR   RefSeq; WP_011282858.1; NC_007292.1.
DR   AlphaFoldDB; Q492Z3; -.
DR   SMR; Q492Z3; -.
DR   STRING; 291272.BPEN_321; -.
DR   PRIDE; Q492Z3; -.
DR   EnsemblBacteria; AAZ40951; AAZ40951; BPEN_321.
DR   KEGG; bpn:BPEN_321; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   BioCyc; CBLO291272:BPEN_RS01580-MON; -.
DR   Proteomes; UP000007794; 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.
FT   CHAIN           1..872
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009297"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           631..635
FT                   /note="'KMSKS' region"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   872 AA;  100838 MW;  DDAEEB6764D24CFC CRC64;
     MRKSYSPSDI ESVVQKHWYK NKTFAVIEDS NKEKYYCLSM IPYPSGNLHM GHVRNYTIGD
     VISRYQRMLG KNVLQPIGWD AFGLPAEHAA IKNNTDPSIW TYSNINYMKS QLQSLGFAYD
     WNRELITCHP DYYRWEQWFF TVLYKKGLVY KKTASVNWCS YHKTVLANEQ VTNNCCWRCH
     TPVKYKRIPQ WFIRITNYAD QLLHGLDQLT HWPEQVKIMQ RNWIGRSKGV NVTFRIENSN
     DTLTIYMTRL DIFMGITYLV ISTDHPIALQ VAKTDLNVAH FIQKNDDFYT KLNKKNVFYF
     EKMGMPTHIY AIHPITNSKL PIWVANFVIP MECDGMGAAI SIPAHNQQDW EFAYKYNLPI
     KPVIKNLDAI EPNIAMQAQE TTCDGILFNS GEFDGLSSCT ASNAIVKSLI ARGVAQYKVN
     YRLKDWGISR QRYWGVPIPM VTLSNGVVKP VLLDRLPVIL PKNMSTIHRS NDGYVDNSLK
     MYPNWIQTTY KGQAAIRDTD TFDTFMESSW YYARYTCPRY NDAMLNVHAA NYWLPVDQYI
     GGIEHAIMHL LYFRFYHKLM RDEGLVYSDE PAIRLLCQGM VLADSFYYVS PNGQHIWVDP
     THVTIKRDRI GGIVKAIDKD GRDLIYDGMC KMSKSKNNGI DPNIIIEKYG ADAVRFFIMF
     AAPIEAPLEW KESGIEGAQR FLKRIWNLIY HHIQDGPVDA LSVVILNHAQ KFIRYNVHKT
     IEKVTDDIDR RQSFNTALSA IMKLVKKLYN APKTSMQDRA VLQEALLVIV RLLYPFTPHI
     SFILWKALGG SEDIDNATWP IVDTQAIQND RTLVLVQING KMRHKVFAPL NSDKNVVYKL
     LETEGVLNKY LIGKKINNII YVPNRVINII AK