ID   SYL_XYLFM               Reviewed;         879 AA.
AC   B0U376;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Xfasm12_1376;
OS   Xylella fastidiosa (strain M12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP000941; ACA12305.1; -; Genomic_DNA.
DR   RefSeq; WP_012337931.1; NC_010513.1.
DR   AlphaFoldDB; B0U376; -.
DR   SMR; B0U376; -.
DR   KEGG; xfm:Xfasm12_1376; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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   Gene3D; 3.90.740.10; -; 1.
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; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 3.
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..879
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091381"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           637..641
FT                   /note="'KMSKS' region"
FT   BINDING         640
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   879 AA;  99798 MW;  9CF661FEC6FCB1C6 CRC64;
     MPTEANTYDP QRIESIAQHY WDSTHAFEVN EHSNKPKYYC LSMLPYPSGA LHMGHVRNYT
     IGDVISRYKR MTGHNVLQPM GWDAFGLPAE NAAIKNKVAP AQWTYKNIER MRTQLKSLGY
     AINWSREFAT CQPDYYVHEQ HMFTRLMRKG LAYRRNALVN WDPVDQTVLA NEQVIDGRGW
     RSGAPVEKRE IPQWFLRITD YAQELLDGLN TLDDWPEPVK TMQRNWIGRS EGLEIRFEVR
     DVDNNALEAL RVFTTRPDTL FGVTFVSIAP EHPLALHAAK SNPGLAGLLT QMKQGGLSEA
     ELKTQEKRGM DTGLKAIHPI TNEQLPVWVA NFVLMAYGTG AVMAVPGHDQ RDQEFANKYG
     LPIRQVIALK EPKNQDESTW EPDVWRDWYA DKTREFELIN SAEFDGLDYQ GAFEVLVERF
     ERQGRGQRRV NYRLRDWGVS RQRYWGCPIP VIYCPTCGAV PVPENQLPVI LPENVAFSGT
     GSPIKTDSEW RKTTCPECGG PAERETDTFD TFMESSWYYA RYTSPNAREM LDKRANYWLP
     VDQYIGGIEH AILHLMYFRF YHKLMRDARL VDSDEPAINL LTQGMVIAET FYRKNPDGSK
     DWINPADVNV ECDERGRITG ATLISDGQPV LIGATEKMSK SKNNGVDPQI MVTKYGADTV
     RLFSMFAAPP EQSLEWNEAG VEGMARFLRR LWTQVHHHAS HGPATALDIT ALDTAQKAIR
     CKTHNTIARV EDDYGRRRSF NTAIAAVMEL SNTLARFDDT TTQSHAVRQE ALETMVLLLN
     PITPHTSHAL WQTLGHPETL LEDLPFPKVD TTALVRETAT LAVQVNGKLR GTIEVATDAP
     REHIENNALT EPNTARFLEG LTVLKIIIVP GKIVNIVAR