ID   SYL_BORA1               Reviewed;         885 AA.
AC   Q2KXE5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 116.
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=BAV2492;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50102.1; -; Genomic_DNA.
DR   RefSeq; WP_012418149.1; NC_010645.1.
DR   AlphaFoldDB; Q2KXE5; -.
DR   SMR; Q2KXE5; -.
DR   STRING; 360910.BAV2492; -.
DR   GeneID; 41394327; -.
DR   KEGG; bav:BAV2492; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001977; 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; 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; Reference proteome.
FT   CHAIN           1..885
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009298"
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;  99022 MW;  A55D8D4B863156EF CRC64;
     MQERYQPNLV EAAAQQDWQA RDAYLVHESA KNADGSEKPK FYACSMLPYP SGKLHMGHVR
     NYTINDMMAR QLRMRGYNVL MPMGWDAFGM PAENAAIKSK VPPAKWTYDN IAYMKKQMKA
     MGLAIDWSRE MCACDPAYYK WNQWLFLKML EKGIAYRKTQ VVNWDPVDQT VLANEQVIDG
     RGWRSGAPVE KREIPGYYLR ITDYADELLD QVKNGLPGWP ERVRVMQENW IGKSEGVRLA
     FPHDIKDENG QLIQDGKLFV FTTRADTVMG VTFCAVAPEH PLATLAARNN PALATFIEQC
     KLGGTTEAEI ATREKEGIPT GLSVKHPLTG QAVDLWVGNY VLMSYGDGAV MGVPAHDERD
     FAFARKYGLT IRQVIAQEGK TYSDQAWQEW YGDKQTGRTI NSGKYDGLST AEAVDAIAAD
     LNALGLGEKQ TTYRLRDWGI SRQRYWGTPI PIIHCQDCGP VPVPEQDLPV VLPDDLIPDG
     SGNPLAKNEA FLSCSCPACG KPARRETDTM DTFVDSSWYF MRYTSPGNDQ AMVDKRNDYW
     MPMDQYIGGI EHAVLHLLYA RFWTKVMRDL GMLKFDEPFT RLLCQGMVLN HIYSRRTPQG
     GIEYFWPEEV ENIYDAKGAI VGARLKSDGS EITYGGVGTM SKSKNNGVDP QSLIDTLGAD
     TARLFVMFAS PPEQTLEWSD SGVDGANRFL RRLWALAYDR RAAVARGLAS GYAWQDAPAP
     VKDLRRELYG LLKQAEYDYQ RIQYNTVVSA SMKMLNAIDN AQLPEGPAAD AAIAEGLGLL
     LRVLYPVVPH VTWHIWRDLG YAAELGDLLD APWPHVDEAA LIADEIELML QVNGKLRGAI
     RVAAQAAKED IEKIAVAQEE VARFLEGRPP KRVIVVPGKL VNVVG
//