ID   SYL_COXBR               Reviewed;         820 AA.
AC   A9NC49;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=COXBURSA331_A0673;
OS   Coxiella burnetii (strain RSA 331 / Henzerling II).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=360115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 331 / Henzerling II;
RA   Seshadri R., Samuel J.E.;
RT   "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT   burnetii isolates.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000890; ABX78122.1; -; Genomic_DNA.
DR   RefSeq; WP_012220266.1; NC_010117.1.
DR   AlphaFoldDB; A9NC49; -.
DR   SMR; A9NC49; -.
DR   PRIDE; A9NC49; -.
DR   KEGG; cbs:COXBURSA331_A0673; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
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; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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..820
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074830"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   820 AA;  94293 MW;  1EF7E8BC8BECDE84 CRC64;
     MNESYQPTLI EQLAQEYWEE NETFEVKEDL SREKFYCLSM LPYPSGDLHM GHVRNYTIGD
     VIARYQIHKG RNVLQPMGWD AFGLPAENAA IQRELPPAEW TRKNIKKMRK QLKQLGFAYD
     WSREITTCDS TYYRWEQWLF LQLYKKGLAY KKNAIVNWDP VDQTVLANEQ IVDGRGWRSG
     AVVERREISQ WFLKITDYSE ELLKDLDELK EWPEQVITMQ RNWIGQSQGV IINFNFEKGP
     DKLQVYTTRP DTLMGVTYLA IAPEHPLAKE RAKKSKKIAA FLKKCKQTRV AEADIATQEK
     EGIDSGLFAV HPLSKEKLPI WIANFVLMEY ASGVVMAVPA HDERDHEFAL KYDLPLKPVI
     EPADGHDWDY NQAAYTNPGK LINSGSFNDI DSKTAFNVIA DYLKNNGAGS RQTHYRLRDW
     GISRQRYWGT PIPIIYCKTC GTVPVPENQL PVLLPEDIIP TGHGSPLKET ASFYKTRCPV
     CNKPATRETD TMDTFVESSW YYARYSCPDQ DKVMLDDRAK YWTPVDQYIG GIEHAVMHLL
     YARFMHKILR DLGLLNSNEP FIRLLTQGMV LKDGAKMSKS KGNVVTPQSL IKKYGADTVR
     LFIIFAAPPE QDLEWSDSGV EGAYRFLKKL WGFSYRIKDA LLAINQQKER SNYQWEAPEH
     RQTRQQIHEC LQQANIDMER LQFNTVVSAV MKILNILIKL TTDNDAEAHL IREGTGILLR
     LLSPITPHIS HHLWQSLGFG GDILDTPWPR PDPKALQTTE LELIVQINGK LRGRIQVPTE
     ASKEIIESTA LNQENVQRHL ADKKIKKVIV VPKKLINIVV