ID   SYL_VIBVY               Reviewed;         857 AA.
AC   Q7MN06;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=VV0911;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC93675.1; -; Genomic_DNA.
DR   RefSeq; WP_011149711.1; NC_005139.1.
DR   AlphaFoldDB; Q7MN06; -.
DR   SMR; Q7MN06; -.
DR   STRING; 672.VV93_v1c08480; -.
DR   EnsemblBacteria; BAC93675; BAC93675; BAC93675.
DR   KEGG; vvy:VV0911; -.
DR   PATRIC; fig|196600.6.peg.915; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002675; Chromosome I.
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; Reference proteome.
FT   CHAIN           1..857
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152116"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           617..621
FT                   /note="'KMSKS' region"
FT   BINDING         620
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   857 AA;  96633 MW;  CB66F2FD342CEF0B CRC64;
     MQEQYNPQDI EQKVQQHWDN NKTFVVTEDP TKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRFQRLQG KNVMQPIGWD AFGLPAENAA VKNNTAPAPW TYENIEYMKN QLKLLGFGYD
     WNREFATCTP EYYRWEQEFF TKLYQKGLVY KKTSSVNWCP NDQTVLANEQ VEDGCCWRCD
     TPVEQKEIPQ WFIKITEYAQ ELLDDLDTLE GWPEMVKTMQ RNWIGRSEGV ELKFEVKGQQ
     DLEVYTTRPD TLMGVTYVGI AAGHPLAKIA AENNPDLAAF IEECKNTKVA EAELATMEKK
     GMATGLTAIH PLNGREVPVY VANFVLMDYG TGAVMAVPAH DQRDFEFATK YGLDIIPVIK
     PIDGSELDIS EAAYTEKGVL FDSGEFDGLE FQAAFDAIAA KLEAEGKGTK TVNFRLRDWG
     VSRQRYWGAP IPMVTTEDGQ VHPVPADQLP VILPEDVVMD GVTSPIKADK EWAKTTFNGE
     PALRETDTFD TFMESSWYYA RYCSPQADDI LDPEKANYWL PVDQYIGGIE HACMHLLYSR
     FFHKLLRDAG YVTSDEPFKQ LLCQGMVLAD AFYYTNDKGG KEWVSPTEVK VERDGKGRIT
     SAVDNEGRNV EHSGMIKMSK SKNNGIDPQE MVDKYGADTV RLFMMFASPA DMTLEWQESG
     VEGANRFLKR VWKLVNEHTS KGAAEAVNAA ALSGDQKALR RDVHKTIAKV TDDVARRQTF
     NTAIAAVMEL MNKLAKAPQE SAQDRAILDE ALKAVVAMLY PITPHICFEM WTALGQQDID
     NASWPTYDEQ ALVEDEKLIV VQVNGKVRGK ITVAADATKE QVEEIGLNEE NVSKHLDGVT
     IRKVIYVPGK LLSIVAN