ID   SYL_THISH               Reviewed;         817 AA.
AC   B8GV13;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=Tgr7_2279;
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7;
RX   PubMed=21475584; DOI=10.4056/sigs.1483693;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL73359.1; -; Genomic_DNA.
DR   RefSeq; WP_012638835.1; NC_011901.1.
DR   AlphaFoldDB; B8GV13; -.
DR   SMR; B8GV13; -.
DR   STRING; 396588.Tgr7_2279; -.
DR   KEGG; tgr:Tgr7_2279; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002383; 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; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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; Reference proteome.
FT   CHAIN           1..817
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199231"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   817 AA;  91879 MW;  4D8F3A4160C9299D CRC64;
     MQEHYEPDAL ERQAQTWWDE HQTFRAREDA PGEPFYCLSM FPYPSGRLHM GHVRNYTIGD
     VISRYQRMQG RNVLQPMGWD AFGLPAENAA IKHLVPPAKW TYENIAYMRG QLQRLGFGYD
     WDRELATCRP EYYRWEQWLF TRLVKKGLAY KKTAMVNWDP VDQTVLANEQ VIDGKGWRSG
     APVERREIPQ WFLRITDYAE ELLKGLDGLE GWPEQVRTMQ RNWIGRSEGV ELEFEVPGEA
     PLTVYTTRPD TLMGVSYVGV APEHPLAARA AEGDGKLAAF IEACRHTKVS EADMATLEKK
     GMDTGLKAVH PVTGEPVPVW VANFVLMEYG TGAVMAVPAH DQRDWEFARQ YGLPVRQVIL
     PAEEGVAVDL DQAAFTDKGV LIESAQFNGL SSAQAFDAIA DFLEKQHKGR RRVNYRLRDW
     GVSRQRYWGC PIPIINCPDC GPVPVPEEQL PVVLPEDVAF DGVGSPIKRM PEFIDTTCPE
     CGGKAERETD TFDTFFESSW YYARYTCKDA DGAMLDERAR HWLPVDQYIG GIEHAVLHLL
     YARFFHKLMR DEGLVDGDEP FTRLLTQGMV LKDGAKMSKS KGNTVDPEAL IERYGADTVR
     LFMMFAAPPE LSLEWSDSGV EGAYRFLKRL WKQVHDHVQG GAAPALDKAA LNADQQALRR
     KLHQTLAKVS DDIGRRTTFN TAIAACMELM NELGRFEDKS GQGRAVMQEA LETTVLMLSP
     IVPHIAHALW SELGREGAAV DQPWPVVDES ALESDTVELV VQVNGKLRAQ IQVPAAAARA
     AIEEAALADE NVQRHIEGKT VVKMVVVPGR LVNVVVK
//