ID   SYL_SALRD               Reviewed;         863 AA.
AC   Q2S415;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 121.
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=SRU_0933;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(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}.
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DR   EMBL; CP000159; ABC46207.1; -; Genomic_DNA.
DR   RefSeq; WP_011403694.1; NC_007677.1.
DR   RefSeq; YP_445066.1; NC_007677.1.
DR   AlphaFoldDB; Q2S415; -.
DR   SMR; Q2S415; -.
DR   STRING; 309807.SRU_0933; -.
DR   EnsemblBacteria; ABC46207; ABC46207; SRU_0933.
DR   KEGG; sru:SRU_0933; -.
DR   PATRIC; fig|309807.25.peg.967; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000008674; 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; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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; 2.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..863
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009423"
FT   MOTIF           42..53
FT                   /note="'HIGH' region"
FT   MOTIF           635..639
FT                   /note="'KMSKS' region"
FT   BINDING         638
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   863 AA;  98948 MW;  DE2DC62AD14854EA CRC64;
     MAYPFHDIET KWQQYWEEHQ TFRTPDEVPD DQEEFYVLDM FPYPSGSGLH VGHPEGYTAT
     DIVARYKRKQ GFNVLHPMGW DAFGLPAEQY ALKTNTHPRE TTEKNIAQFK RQLKRLGFSY
     DWQREINTTD PDYYKWTQWI FLQLYEKGLA YQSEEPVWWC EELGTVLANE EVIDGKSERG
     GYPCERVPMR QWVLKITEYA DRLLEGLEDL DWPESTKEMQ RNWIGRSEGA NVYFDLVGAD
     DALEVYTTRP DTLFGATYMV LAPEHELLDE ITTDEHREDV DEYCRQALRK SERKRQQQGD
     KTGVFTGGYA VNPVNGEEIP IWVADYVLVS YGTGAIMAVP AHDERDHAFA NKYDLPIREV
     VEGGDIDEEA YTGDGPHVHS ANEAVSLNGL RNEEAKEAIT EWLDEEEKGE RTVNYQLQDW
     LFSRQRYWGE PFPIVFTEDG EDKPVPEEEL PVTLPDLDVF EPSGTPEGPL ATIEDWRETT
     DPETGEPAQR ETNTMPQWAG SCWYYLRFID PDNDEQLVDP EKEEYWMPVD LYVGGSEHAV
     LHLLYARFWH KVLYDAGVVS TKEPFQTLVH QGMILGETEY TAYRDDAGEF VSAEQVDDDA
     DLTPVPVDDG DVKKDGDVFV LADRPAVRVD ARSHKMSKSR GNVINPDDVV DEYGADTLRL
     YEMFMGPLEQ DKPWSTDDME GVHRFLNRIW RLVVDADSGG LAVSDEEPDR EQLRTLHRTI
     KTVTEDIEAR DFNTAIAAMM EFVNAANKWD ALPRQVATPF VLLLSPFAPH LAEELWARLG
     HDQSLAYADW PAYDDELIRR EVVEMPVQVD GTVRATIEVA ADAEEADVLA TAKEAENVAR
     HLDDEDLQRE IYVPGQIVNF VTG
//