ID   SYL_BORBR               Reviewed;         885 AA.
AC   Q7WH33;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=BB3377;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640447; CAE33869.1; -; Genomic_DNA.
DR   RefSeq; WP_010926800.1; NC_002927.3.
DR   AlphaFoldDB; Q7WH33; -.
DR   SMR; Q7WH33; -.
DR   STRING; 257310.BB3377; -.
DR   EnsemblBacteria; CAE33869; CAE33869; BB3377.
DR   GeneID; 66437925; -.
DR   KEGG; bbr:BB3377; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001027; 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; 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   PANTHER; PTHR43740; PTHR43740; 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; 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..885
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151979"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           639..643
FT                   /note="'KMSKS' region"
FT   BINDING         642
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   885 AA;  99008 MW;  CA58CA2663A754DF CRC64;
     MQERYQPNSV EAAAQQTWQA RDAYLVHEHA KNPDGSEKPK FYACSMLPYP SGKLHMGHVR
     NYTINDMMAR QLRMRGYNVL MPMGWDAFGM PAENAAIKSK VPPAKWTYDN IAYMKKQMKA
     MGLAIDWSRE MCACDPKYYK WNQWLFLKML EKGIAYRKTQ VVNWDPVDQT VLANEQVIDG
     RGWRSGAPVE KREIPGYYLR ITDYAEELLD QVSTNLPGWP ERVRLMQENW IGKSEGLRFA
     FPHRIAGADG KLIQDGKLYV FTTRADTIMG VTFCAVAPEH PLATHAAQSN PALAAFVEQC
     KLGGTTEAEM ATREKEGMPT GLTVTHPLTG AEIDVWVGNY VLMTYGDGAV MGVPAHDERD
     FAFARKYGLP IRQVVALEGK TYSTDAWQEW YGDKQAGRTV NSGKYDGLAY QAAVDTIAAD
     LAAQGLGEKQ TTWRLRDWGI SRQRYWGTPI PIIHCADCGP VPVPEQDLPV VLPDDLIPDG
     SGNPLAKNEA FLSCSCPRCG KPARRETDTM DTFVDSSWYF MRYTSPDNDQ AMVDARNDYW
     MPMDQYIGGI EHAVLHLLYA RFWTKVMRDL GLLNFDEPFT KLLCQGMVLN HIYSRKTPQG
     GIEYFWPEEV DNVYDAKGAI VGAKLQRDGS EVNYGGVGTM SKSKNNGVDP QSLIDTLGAD
     TARLFVMFAS PPEQTLEWSD SGVEGANRFL RRLWALGYAQ REAVGRGLAT GADWAQAPAP
     VKELRREVYG LLKQADYDYQ RIQYNTVVSA CMKMLNAIDD APLPEGPAAD AARAETLGLL
     LRVLYPVVPH ITWHLWQDLG YAEHLGDLLD APWPHVDEAA LVADEIELML QVNGKLRGSI
     RVAAKAPKED IERIAAAQEE VARFLEGRPP KRVIVVPGKL VNVVG