ID   SYL_BARQU               Reviewed;         880 AA.
AC   Q6FYL6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=BQ12310;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF26690.1; -; Genomic_DNA.
DR   RefSeq; WP_011179859.1; NC_005955.1.
DR   AlphaFoldDB; Q6FYL6; -.
DR   SMR; Q6FYL6; -.
DR   KEGG; bqu:BQ12310; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000597; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 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; 2.
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..880
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151976"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   880 AA;  99339 MW;  135ECA8B81E0C70E CRC64;
     MTIEHSNVGE RYNPRAREQK WQAIWDEKKI FQITEENCRE KYYVLEMFPY PSGRIHMGHV
     RNYTMGDVVA RYKRAKGFDV LHPMGWDAFG MPAENAALQS KVHPKTWTYQ NIAVMRGQLK
     QLGLSLDWSR EFATCDVAYY HRQQMLFLDL YQKGLVARKV AKVNWDPVDQ TVLANEQVVD
     GCGWRSGALV EQRELAQWFF KISDFSEDLL AGLEELEQWP EKVRTMQKNW IGKSQGLLIR
     WALKSTNGAD EVCEAFNEVV CYSTRPDTLF GASFLALSVD HPISQALAQK DKALSAFIEN
     CRCGGMTTAA LETAEKQGFC TSLLAVHPFN PRIHLPVYIA NFVLMDYGTG AVFGCPAHDQ
     RDWDFAHKYD LPVQPVVLPK GSDAEDFVIA ETPYTGDGVM INSDFLDGLT PQEAFEAAAE
     RLEGQMLNGQ PQGKRTVQFR LRDWGISRQR YWGCPIPIIH CAACGVVPVP RADLPVELPD
     DVTFDQPGNP LERHEKWQKV ACPVCGQSAK RETDTMDTFV DSSWYYARFT APWAQEPVDK
     NAIAEWLPVQ QYIGGIEHAI LHLLYARFFM RAMKLIGYVT VDEPFKGLFT QGMVVHETYR
     DDQGWVSPAE ISIIEKDGKR QAHKLTDQSE VTIGLIEKMS KSKKNVVDPD DIIASYGADT
     VRWFVLSDSP PERDVIWTES GVEGAYRFVQ RVWRCVVLSA PVLKEVIPCT GHQGAALELS
     KAAHRMLCTV EDDLEKFAFN RAIARLYEFL NIMAPLLNKI ASVEDEMKAS LRQAMDFFLA
     LIAPIMPHLA EECHAALGGK TLICELPWPV YDPALIVEDC CTLPVQINGK KRGEVTVAAT
     ASEAMIEEAV LALDFVQAHL VEKSIKKMII VPQRIVNVVL
//