ID   SYL_BORPD               Reviewed;         885 AA.
AC   A9HWW6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Bpet3324;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP43666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9HWW6; -.
DR   SMR; A9HWW6; -.
DR   STRING; 94624.Bpet3324; -.
DR   PRIDE; A9HWW6; -.
DR   EnsemblBacteria; CAP43666; CAP43666; Bpet3324.
DR   KEGG; bpt:Bpet3324; -.
DR   eggNOG; COG0495; Bacteria.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001225; 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; Reference proteome.
FT   CHAIN           1..885
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334733"
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;  98772 MW;  DF3BBA0AF1F0EFE2 CRC64;
     MQERYSPTAV EAAAQQDWQA RDAYRVTEHA RNADGTEKPK FYACSMLPYP SGKLHMGHVR
     NYTINDMMAR QLRMRGYNVL MPMGWDAFGM PAENAAIKSK VPPAKWTYDN IAYMKKQMQA
     MGLAIDWSRE MCACDPEYYK WNQWLFLKML EKGIAYRKTQ VVNWDPVDQT VLANEQVIDG
     RGWRSGALVE KREIPGYYLR ITDYADELLD QVRSGLPGWP ERVRAMQENW IGKSEGVRFA
     FPHTIAGADG QLIQDGRLYV FTTRADTIMG VTFCAVAPEH PLATHAAATN PELASFIEQC
     KLGGTTEAEI ATREKAGMRT GLTVTHPLTG APVDVWVGNY VLMSYGDGAV MGVPAHDERD
     FAFAKKYQLP IRQVVAHEGK AYSTDAWQEW YGDKQGGRTV NSGKYDGLPY AEAVDAIAAD
     LAAQGLGEKQ TTWRLRDWGI SRQRYWGTPI PIIHCADCGP VPVPEQDLPV VLPDDLIPDG
     SGNPLAKNEA FLSCSCPRCG KPARRETDTM DTFVDSSWYF MRYTSPGNDQ AMVDARNDYW
     MPMDQYIGGI EHAVLHLLYA RFWTRVMRDL GLLKFDEPFT KLLCQGMVLN HIYSRKNAQG
     GIEYFWPEEV ENLYDAKGAI TGARLKSDGS DVNYGGVGTM SKSKNNGVDP QALIDTLGAD
     TARLFVMFAS PPEQTLEWSD SGVEGANRFL RRLWSHCHAH RDAVARGLAA GADWAQAPAP
     VKDLRREVYG LLKQADYDYQ RIQYNTVVSA CMKMLNAIDD AKLPEGAHAD AARAETLGVL
     LRVLYPVVPH VTWLLWRELG YTHSLGDLLD APWPHVDEAA LVADEIELML QVNGKLRGAI
     RVAAKASKAD IEQIAAAQEE VARFLEGRPP KRVIVVPGKL VNVVG