ID   SYL_LEGPL               Reviewed;         823 AA.
AC   Q5WWZ8;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 110.
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=lpl1301;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(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; CR628337; CAH15541.1; -; Genomic_DNA.
DR   RefSeq; WP_011215377.1; NC_006369.1.
DR   AlphaFoldDB; Q5WWZ8; -.
DR   SMR; Q5WWZ8; -.
DR   KEGG; lpf:lpl1301; -.
DR   LegioList; lpl1301; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   Proteomes; UP000002517; 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; 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; 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.
FT   CHAIN           1..823
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152033"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           575..579
FT                   /note="'KMSKS' region"
FT   BINDING         578
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   823 AA;  94078 MW;  1A38EBB26154BA4F CRC64;
     MDNTYNPQEV EEQAQQYWHK KQSFNVTEDL NKEKFYCLSM FPYPSGTLHM GHVRNYTLGD
     VIARYQRALG KNVLQPIGWD SFGLPAENAA IKNKIPPAEW TRKNIAAMKE QFLRLGNAYD
     WKREITTCDP EYYRWEQWFF IRLFEKGLVY KKNAVVNWDP VDQTVLANEQ VVDGRGWRSG
     ALVERKEISQ WFIKITSYAD ELLSSLDSLD EWPAQVKQMQ RNWIGKSIGT EIYFNVNNYP
     KRLKIYTTRP DTLMGATYLA VATDHPLAKE AASNNKKVQE FLDSCQGIKI AEAELATMEK
     RGIDTGMTAI HPITGKELPI WVANFVLMQY GSGAVMAVPA HDQRDWEFAQ KYQLPVKQVI
     KPIGIEHDFN QSAYTEEGIL INSNQFDNLL SSKAIQVITN FLEENDAGKA TINYRLRDWG
     VSRQRYWGTP IPMIICEQCG IVPVPDEELP VVLPENVDFT GTGSPLTQCK EFVNITCPKC
     GQDATRETDT FDTFVESSWY YARFACKGQE NAMLDDRAKY WTPVDQYIGG IEHAVMHLLY
     ARFFHKLMRD EGLVNSDEPF KALLTQGMVL KDGHKMSKSL GNVVDPNHLI NTYGADTARL
     FVMFASPPEQ SLEWSDSGVE GAHRFLKRVW AFSHQHRDML IDINDSILSG NGHVDWKEAE
     SRLKKSRHIV HQILAQATHD YDRNQFNTVV SGCMKLFNEI SDYSIETEND KFFIHSSISI
     LLRLLAPITP HICHCLWQQL GFDKAIIDAP WPKVDKSALK TDEVDYVVQV NGKLRAQFTA
     STDATEEELI AAAKEHAHNF VVNHTIKKAI IVPHRQLINL VIG
//