ID   SYL_VIBA3               Reviewed;         858 AA.
AC   B7VKF7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=VS_0718;
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32;
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) 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; FM954972; CAV17713.1; -; Genomic_DNA.
DR   RefSeq; WP_012603379.1; NC_011753.2.
DR   AlphaFoldDB; B7VKF7; -.
DR   SMR; B7VKF7; -.
DR   STRING; 575788.VS_0718; -.
DR   EnsemblBacteria; CAV17713; CAV17713; VS_0718.
DR   KEGG; vsp:VS_0718; -.
DR   PATRIC; fig|575788.5.peg.2066; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000009100; Chromosome 1.
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   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..858
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199233"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           618..622
FT                   /note="'KMSKS' region"
FT   BINDING         621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   858 AA;  96921 MW;  B3F6DA3F0E43E9A9 CRC64;
     MQEQYNPQEI EQKVQQHWDD SETFVVSEDP NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRFQRLQG KNVMQPIGWD AFGLPAENAA VKNNTAPAPW TYENIEYMKN QLKLLGFGYD
     WKREFATCTP EYYRWEQEFF TKLYEQGLVY KKTSSVNWCP NDQTVLANEQ VEDGCCWRCD
     TPVEQKKIPQ WFIKITEYAQ ELLDDLDNLE GWPEMVKTMQ RNWIGRSEGV ELSFAVNGEE
     APLEVYTTRP DTLMGVSYVG IAAGHPLAEK ASKNNPELAA FVEECRNTKV AEAELATMEK
     KGMDTGLTAI HPLNGRVVPV YVANFVLMDY GTGAVMAVPA HDQRDYEFAT KYGIDIIPVI
     KPEDGSELDV SEAAYTEKGV LFDSGEFDGL AFQEAFDAIA AKLEAEGKGK KTVNFRLRDW
     GVSRQRYWGA PIPMVTTEDG EVHPVPADQL PVILPEDVVM DGVTSPIKAD KSWAETTFNG
     EPALRETDTF DTFMESSWYY ARYCSPQADD ILDPEKANYW LPVDQYVGGI EHACMHLLYS
     RFFHKLLRDA GYVTSDEPFK QLLCQGMVLA DAFYHENEKG TKEWIAPTDV TVERDGKGRI
     EKAVDDQGRE VEHSGMIKMS KSKNNGIDPQ EMVDKYGADT VRLFMMFASP ADMTLEWQES
     GVEGANRFLK RVWKLVHAHS SKGAAETVDA SALSGNQKAL RRDIHKTIAK VTDDIGRRQT
     FNTAIAAIME LMNKLAKAPQ ESVQDRAILD EALKAVVRML YPMTPHISYE MWIALGESNV
     DSATWPTFDE KALVEDEKTI VVMINGKLRA KLTVAADATE EQVRELGLND ENAKKFLDGL
     TIRKVIFVPG KLLNIVAN