ID   SYL_SHEB9               Reviewed;         859 AA.
AC   A9L001;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   27-MAR-2024, entry version 90.
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=Sbal195_3447;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABX50609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000891; ABX50609.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_006086959.1; NC_009997.1.
DR   AlphaFoldDB; A9L001; -.
DR   SMR; A9L001; -.
DR   GeneID; 11773495; -.
DR   KEGG; sbn:Sbal195_3447; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   Proteomes; UP000000770; 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; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; 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.
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.
FT   CHAIN           1..859
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334815"
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   859 AA;  96596 MW;  28FDE3FEAEF8BC5F CRC64;
     MQEQYNPSEI EALVQKHWHD NKTFEVTEDA NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VVARFQRLQG KNVLQPIGWD SFGLPAENAA INNKTAPAPW TYENIEYMKN QLKLLGFGYD
     WSREIATCTP EYYRWEQWFF TKLYEKGLVY KKTASVNWCP NDETVLANEQ VQDGCCWRCD
     TPVEQKEIPQ WFIKITAYAE ELLNDIDTLD GWPDQVKTMQ RNWIGRSEGV EMTFGVAGHD
     KSFDIYTTRP DTLMGVTYVA IAAGHPLAEI AAQTNPELAA FIDECKNSTT SEAELATMEK
     RGVATGLFAI HPITGKQVPI WAANFVLMNY GTGAVMSVPG HDQRDFEFAK KYGLAIEAVI
     KPVDGDVDIS EAAYTEKGVL FNSGEFDGLD FEAGFNAIAN KLVAEGKGKR QVNYRLRDWG
     VSRQRYWGAP IPMVTLADGT VIPTPADQLP VLLPEDVVMD GIQSPIKADK EWAKTQVNGQ
     DALRETDTFD TFMESSWYYA RYCSPHADEM LDPAKANYWL PVDQYIGGIE HACMHLLYFR
     FFHKLLRDAG LVNSNEPAKQ LLTQGMVLAD AFYYINEKGA RVWVSPLDVA TTEKDDKGRI
     TKAIDKDGNE LVYTGMSKMS KSKNNGIDPQ VMVEKYGADT VRLFMMFASP PELTLEWQES
     GVEGAHRFIK RLWKLANEHV NQDNSEALDA SKLTSDQKAL RREVHKTIAK VTDDIGRRQM
     FNTAVAAVME LMNHLQKAPQ TTGQDNAIIG EALSAIVRLL YPIIPHVSFN LWNELGNASN
     IEDSQWPVVD EAALVEDSKL IVVQVNGKVR AKITVAADAD KESVEALGMS DEHVIKYLDG
     LTVRKVIYVP GKLLSIVAN
//