ID   SYL_BDEBA               Reviewed;         796 AA.
AC   Q6MQU3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=Bd0365;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX842646; CAE78015.1; -; Genomic_DNA.
DR   RefSeq; WP_011162956.1; NC_005363.1.
DR   AlphaFoldDB; Q6MQU3; -.
DR   SMR; Q6MQU3; -.
DR   STRING; 264462.Bd0365; -.
DR   PRIDE; Q6MQU3; -.
DR   EnsemblBacteria; CAE78015; CAE78015; Bd0365.
DR   KEGG; bba:Bd0365; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; DIDWADV; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008080; 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; 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; 2.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..796
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151977"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           569..573
FT                   /note="'KMSKS' region"
FT   BINDING         572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   796 AA;  89437 MW;  01B10754DBB8D8A5 CRC64;
     MSLNFTEYEA KWQKKWADAK AFQAETTSSK PKYYALDMFP YPSASGLHVG HMASYTPGDI
     ISRYKRVNGF NVLHPMGYDA FGLPAEQYAI QTGVHPAITT KKAIDSFRKT LQTFGFSFDW
     SREISTCEPD YYKWTQFIFL KLYERGLAYQ KEVPVNWCPA LKTVLANDEV VDGKSERGGH
     PVIRVPMKQW MLKITDYAER LLNDLDKLDW PERTKEGQRN WIGKSEGARI TFKVHGEKDT
     FEVFTTRPDT LFGVTFMVMA PEHPLVKKIT SQPQYTAVEN YIADTAKKSE VDRKASTEKT
     GVFTGAHATH PITGDKIEIW ISDYVLMDYG TGAIMAVPGH DARDFEFATK FNIPIKSVLE
     SDMLPFEGDS IMINSEFLDG LNKTEAISKM LKHLEENKLG VREVQYKLRD WLFSRQRYWG
     EPFPIVHFAD GSKGVPVNEL PVILPEVADY EPADTGEAPL ARNADWVKYM DGDKEGRRET
     DTMPGAAGSS WYFLRYIDPK NTEAPFSPEA EKYWMPVDLY VGGPEHTVGH LLYARFWTKV
     LFDCGLVTHD EPFQKLAHQG MILGPDGEKM SKSRGNVISP EDIARSHGAD ALRTFISFMG
     PVDKDKPWAP TGIDGVKRFL DRITRLVVND DGQLVATSEA LTPEIEKLVH KTIKKVTEDI
     ESMSFNTAIS AMMILVNELY RAECRSVLAV KPLVQILAPF APHLAEELWE KMNGEGLCAL
     APWPKYDNTL CADDTVTIGV QVNGKMRGTI EIGVAASEQE AVAAAKAVQQ VAAVLGDKNP
     DKVIYKAGKI LNLIVK