ID   SYL_WOLPM               Reviewed;         838 AA.
AC   Q73IT7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=WD_0060;
OS   Wolbachia pipientis wMel.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=163164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA   Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA   McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA   Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA   Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA   Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA   O'Neill S.L., Eisen J.A.;
RT   "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT   streamlined genome overrun by mobile genetic elements.";
RL   PLoS Biol. 2:327-341(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; AE017196; AAS13823.1; -; Genomic_DNA.
DR   RefSeq; WP_010962340.1; NZ_OX384529.1.
DR   AlphaFoldDB; Q73IT7; -.
DR   SMR; Q73IT7; -.
DR   EnsemblBacteria; AAS13823; AAS13823; WD_0060.
DR   GeneID; 70035550; -.
DR   KEGG; wol:WD_0060; -.
DR   eggNOG; COG0495; Bacteria.
DR   Proteomes; UP000008215; 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; 3.40.50.620; 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..838
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152118"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT   MOTIF           611..615
FT                   /note="'KMSKS' region"
FT   BINDING         614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   838 AA;  95661 MW;  81D296221BF255A8 CRC64;
     MKYDFKSVEK FYQDKWDFSV SKSGKQEKCY VLEMFPYPSG KIHMGHLRNY AIGDVIARYK
     RANGFEVLHP IGWDAFGLPA ENAARDNNIS PETWTKENID NMRTQLKSIG LSYNWERELS
     TCEPDYYKHE QKFFLDFLKH GLAYRKESWV NWDPVDQTVL ANEQVVDGKG WRSGAVVEKR
     KLSQWFLKIT DFAEDLLKCL QSLKNWPEKV KTMQERWIGK SEGATIEFEV VGLNKKLKVF
     TTYPHTLFGA SFCAVAAEHP IVQDLKNGSS VVIPVLDTGI QEIKSKREND EKIGVYTGLN
     VKHPFLDKEL PLYIANFVLM EYGEGAIFGC PAHDQRDFEF AQKYNLPIIP VISSAHLGVI
     PARDQNSYNG SQCQATQMTK EAYTGDGTMF NSEFLNGLMV SEAKEAIVKK FEEKKIGKKT
     INYRLHDWGV SRQRYWGCPI PIIYCKDCGT VPVPEKDLPV VLPIDVEFTS GGNPLDKHPT
     WKFVDCPKCG KQAERETDTF DTFFESSWYF AAFCSEDKSI DKDACNRFMP VDYYIGGIEH
     AILHLLYSRF FCRALTKCGY FDIKEPFSTL ITQGMVCHAT YKDENGKWLF PAEAKELIAR
     GAKVQVGKVE KMSKSKKNTV DPNFIIEKYG ADTARLFVLS DTPPEKDMEW SDDGVEGCSR
     YVNKLWRMVM QLRPVNIHYD NENVTGGLLE YRKKIHKLLH GLTDDLENCR LNCVVAKFRE
     MTNLIAEIDV KTGKSLIDEG ICILIRVIEP FIPHLAESLW QEIGGQPWPK ADESLLVDDT
     VTIAVQINGK LRTTIKVAIN LPQEELKKIA IDSVSSKIDQ SKVRTVYAVP NKIVNIVI
//