ID   SYL_BLOFL               Reviewed;         867 AA.
AC   Q7VRA6;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=Bfl313;
OS   Blochmannia floridanus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(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; BX248583; CAD83383.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7VRA6; -.
DR   SMR; Q7VRA6; -.
DR   STRING; 203907.Bfl313; -.
DR   KEGG; bfl:Bfl313; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002192; 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..867
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151994"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           625..629
FT                   /note="'KMSKS' region"
FT   BINDING         628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   867 AA;  101320 MW;  B8A6FB76B78356C9 CRC64;
     MKKLYFPHQI ERIVQQHWND NQTFSVTEDK NKQKFYCLSM LPYPSGNLHM GHVRNYTIGD
     VISRYQRMLG KNVLQPIGWD AFGLPAEQAA IIHKKNPSDW TYSNIQYMKQ QLKSLGFAYD
     WKRELITNDP QYYRWEQWFF IILYEKGLVY RKTTLVNWCP YHNTVLANEQ VINGGCWRCH
     TKIQYKKIPQ WFIKITHYAD QLLNGLNQLQ YWPEQVKTMQ RNWIGQSTGT NVIFKILNSN
     ITTITVYIAR LDTFMGISYL TISVDHPITL QIAKINPDLA NFISIYNTIS IQLHNKQFIC
     HKKKGIFTNL YAVHPITFTK LPIWVANFIT PLEFDGQGAI ASCPAHDQHD WEFAHQYDLP
     IKPVIKYADG ELPNITNQAM IEPGILFNSD NFDDLTSHTA INYISKKLID LKIAKTKIFY
     HLQDWGVSRQ RYWGVPIPMI KLKNGIIQPV PKSELPVILP EIIYTKNNEN NILSKNFNWT
     HTTYKNQDVI RDTDTFDTFM ESSWYYARYT CPHYHDGMLQ SDAANYWLPI DQYIGGIEHA
     TMHLMYFRFY HKLMRDIGLI QSNEPAIRLL CQGMILADSF YYISNDGQKN WVSPNKVIST
     RDKMGHIIKS IDADGNNVIY AGLCKMSKSK NNGIDPNAMI QKYGADAVRF FIMFAAPAHS
     TLEWKESGIE GALRFLKRLW NITYQHIQNG LIHQLNMYKL ENKHKIIRQK VHETIIKVTD
     DIDRRQSFNT ALAAIMKLFN DIQDIFPINN TQDRSVLHEA LSIIVKLLYP FTPHISYILW
     KELGYTNTID DTTWPTPDLQ AIQTQEILII VQINGKKKKK IFVPINSDKN TIHEIAKQAI
     YQDKNLESKY VHKIIYIPNK IINFITK
//