ID   SYL_LEGPA               Reviewed;         823 AA.
AC   Q5X5L8;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=lpp1302;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
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; CR628336; CAH12453.1; -; Genomic_DNA.
DR   RefSeq; WP_011213647.1; NC_006368.1.
DR   AlphaFoldDB; Q5X5L8; -.
DR   SMR; Q5X5L8; -.
DR   KEGG; lpp:lpp1302; -.
DR   LegioList; lpp1302; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
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; 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; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 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.
FT   CHAIN           1..823
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152031"
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;  94105 MW;  53069F3A8F74E132 CRC64;
     MDNTYNPQEV EEQAQQYWHK KQSFNVTEDL NKEKFYCLSM FPYPSGTLHM GHVRNYTLGD
     VIARYQRALG KNVLQPIGWD AFGLPAENAA 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
     KPIDIEHDFN QSAYTEEGIL INSNQFDNLL SSKAIQVITN FLEENDAGKA TINYRLRDWG
     VSRQRYWGTP IPMIICEQCG IVPVPDEELP VVLPENVDFT GTGSPLTQCK EFVNVTCPKC
     GQDANRETDT 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
     STDASEEELI AAAKEHAHNF VVNHTIKKAI IVPHRQLINL VIG