ID   SYL_PHOPR               Reviewed;         858 AA.
AC   Q6LN98;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=PBPRA2885;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR378672; CAG21228.1; -; Genomic_DNA.
DR   RefSeq; WP_011219500.1; NC_006370.1.
DR   AlphaFoldDB; Q6LN98; -.
DR   SMR; Q6LN98; -.
DR   STRING; 298386.PBPRA2885; -.
DR   PRIDE; Q6LN98; -.
DR   EnsemblBacteria; CAG21228; CAG21228; PBPRA2885.
DR   KEGG; ppr:PBPRA2885; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000593; 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   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..858
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152061"
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;  97148 MW;  869C4DFBD581B4E0 CRC64;
     MQEQYRPQDI EQKVQEHWDN NKTFVVNEDP NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRYQRLQG KNVMQPIGWD AFGLPAENAA VKNKTAPAPW TYENIEYMKN QLKLLGFGYD
     WSREFATCTP EYYRWEQEFF TKLYNKGLVY KKTSSVNWCP NDQTVLANEQ VEDGCCWRCD
     TPVEQKKIPQ WFIKITEYAQ ELLDDLDTLD GWPEMVKTMQ RNWIGRSEGV ELSFAVNGEE
     APLEVYTTRP DTLMGVTYVG IAAGHPLAEK AAATNPELFA FTEECRNTKV AEAELATMEK
     KGMDTGLRAV HPLNGREVPI YVANFVLMDY GTGAVMAVPA HDQRDYEFAT KYGLDIIPVI
     KPEDGSELNV SEEAYTEKGV LFDSGEFDGL AFQDAFDAIA AKLEAEGKGK KTVNFRLRDW
     GVSRQRYWGA PIPMVTTEDG EVHPVPADQL PVILPENVVM DGVTSPIKAD KEWAKTTFNG
     EPALRETDTF DTFMESSWYY ARYCSPQADD ILDPEKANYW LPVDQYVGGI EHACMHLLYS
     RFFHKLLRDA GYVTSNEPFK QLLCQGMVLA DAFHHTNEKG TKEWIAPTDV TIERDAKGRI
     EKAIDDQGRE VQHSGMIKMS KSKNNGIDPQ EMVDKFGADT VRLFMMFASP ADMTLEWQES
     GVEGASRFLK RVWKLVHEHT NKGTVEALDV AALSGNQKAL RRDVHKTIAK VSDDIGRRQT
     FNTAIAAIME LMNKLNKAPQ ESAQDRALLD EALKAVVVML YPMTPHASFE MWEALGETDI
     DTATWPTFDK NALIEDEKTI VVMINGKLRA KLIVAADATE EQVKELGLKD ENAIKFLDGL
     TIRKVIYVPG KLLNIVAN