ID   SYL_LEGPC               Reviewed;         823 AA.
AC   A5IBJ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=LPC_0764;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000675; ABQ54741.1; -; Genomic_DNA.
DR   RefSeq; WP_011946380.1; NC_009494.2.
DR   AlphaFoldDB; A5IBJ1; -.
DR   SMR; A5IBJ1; -.
DR   KEGG; lpc:LPC_0764; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
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_1000009363"
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;  5FC46C70F62FD9E9 CRC64;
     MDNTYNPQEV EEQAQQYWHK KQSFNVTEDL NKEKFYCLSM FPYPSGTLHM GHVRNYTLGD
     VIARYQRALG KNVLQPIGWD AFGLPAENAA IKNKIPPAEW TRKNIAAMKE QFLRLGNAYD
     WKRELTTCDP 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
//