ID   SYL_LEGPH               Reviewed;         823 AA.
AC   Q5ZVU2;
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=lpg1348;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(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}.
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DR   EMBL; AE017354; AAU27430.1; -; Genomic_DNA.
DR   RefSeq; WP_010947078.1; NC_002942.5.
DR   RefSeq; YP_095377.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZVU2; -.
DR   SMR; Q5ZVU2; -.
DR   STRING; 272624.lpg1348; -.
DR   PaxDb; Q5ZVU2; -.
DR   PRIDE; Q5ZVU2; -.
DR   EnsemblBacteria; AAU27430; AAU27430; lpg1348.
DR   GeneID; 66490480; -.
DR   KEGG; lpn:lpg1348; -.
DR   PATRIC; fig|272624.6.peg.1418; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000609; 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; 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.
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..823
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152032"
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;  94106 MW;  6CA16AB4D05B6F5D 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
     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