ID   SYL_BARHE               Reviewed;         880 AA.
AC   Q6G1W2;
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=BH15390;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / CCUG 30454 / Houston
OS   1) (Rochalimaea henselae).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / CCUG 30454 / Houston 1;
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; BX897699; CAF28302.1; -; Genomic_DNA.
DR   RefSeq; WP_011181305.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q6G1W2; -.
DR   SMR; Q6G1W2; -.
DR   PaxDb; 283166-BH15390; -.
DR   EnsemblBacteria; CAF28302; CAF28302; BH15390.
DR   KEGG; bhe:BH15390; -.
DR   eggNOG; COG0495; Bacteria.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000421; 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   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_0000151975"
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;  100077 MW;  5589AC710AB5F1B8 CRC64;
     MTIEHYNLGE RYNPRACERK WQAIWDEKKT FQTVQEDRRE KYYVLEMFPY PSGRIHMGHV
     RNYAMGDVVA RYKRAKGFNV LHPMGWDAFG MPAENAAMQN KVHPKTWTYQ NIAVMRGQLK
     QLGLSVDWSR EFATCDVDYY HRQQMLFLDF YQKGLVARKV AKVNWDPVDQ TVLANEQVVD
     GRGWRSGALV EQRELTQWFF KISDFSEDLL AGLEELEQWP EKVRIMQKNW IGKSQGLLIR
     WALKSTEEAD EVCKSFDEVV CYSTRPDTLF GASFLALSVD HPLAQALAQK DKALEFFIEN
     CRSGGTTTAE LETAEKQGFR TSLVAVHPFD VAVHIPVYIA NFVLMDYGTG AVFGCPAHDQ
     RDFDFARKYD LPVQPVVLPS GVEREDFAIT ETPYLGDGVM INSSFLDGLT PQQAFEEAAK
     RLEGQMLNGK PQAEKTVQFR LRDWGISRQR YWGCPIPMIH CTSCGVVPVP RADLPVVLPD
     DVTFEQPGNP LVCHETWKSV ACPVCGQFAK RETDTMDTFV DSSWYYARFT APFAQEPVDK
     KATTEWLPVQ QYIGGIEHAI LHLLYARFFT RAMKSMGYVT VDEPFKGLFT QGMVVHETYR
     DEKDWVSPEE ISIVEKDGKR QAYKLTDQSE VTIGSIEKMS KSKKNVVDPD DIIASYGADT
     VRWFILSDSP PERDVIWTES GVEGAHRFVQ RVWRCVALSA PVLRDVVPCV GKQGAALQLS
     KVAHRTLYAV EDDLEKFAFN RAIARLYEFL NIMAPLLNRI ENVEDEMKAA LRQAMDFFLA
     MIAPIMPHLA EECHAALGEK TLISELAWPV CDRALTVEEC YTLPVQINGK KRGEVTVAAT
     ASEAMIEEAV LALDFVKVHL VKKPVKKMII VPKRIVNVVL
//