ID   SYL_COXB2               Reviewed;         820 AA.
AC   B6J1B2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, 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=CbuG_1438;
OS   Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CbuG_Q212;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(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; CP001019; ACJ18740.1; -; Genomic_DNA.
DR   RefSeq; WP_012570259.1; NC_011527.1.
DR   AlphaFoldDB; B6J1B2; -.
DR   SMR; B6J1B2; -.
DR   KEGG; cbg:CbuG_1438; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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_1000091310"
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;  94273 MW;  06B683979B235DCF CRC64;
     MNESYQPTLI EQLAQEYWEE NETFEVKEDL SREKFYCLSM LPYPSGDLHM GHVRNYTIGD
     VIARYQIHKG RNVLQPMGWD AFGLPAENAA IQRELPPAEW TRKNIKKMRK QLKQLGFAYD
     WSREITTCDS TYYRWEQWLF LQLYKKGLAY KKNAIVNWDP VDQTVLANEQ IVDGRGWRSG
     AVVERREISQ WFLKITDYSE ELLKDLDELK EWPEQVITMQ RNWIGQSQGV IINFNLEKGP
     DKLQVYTTRP DTLMGVTYLA IAPEHPLAKE RAKKSKKIAA FLKKCKQTRV AEADIATQEK
     EGIDSGLFAV HPLSKEKLPI WIANFVLMEY ASGVVMAVPA HDERDHEFAL KYDLPLKPVI
     EPADGHDWDY NQAAYTNPGK LINSGSFNDI DSKTAFNLIA 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
//