ID   SYL_SHEPA               Reviewed;         859 AA.
AC   A8H7C2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 85.
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=Spea_3143;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
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., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-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=ABV88459.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000851; ABV88459.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041411594.1; NC_009901.1.
DR   AlphaFoldDB; A8H7C2; -.
DR   SMR; A8H7C2; -.
DR   STRING; 398579.Spea_3143; -.
DR   EnsemblBacteria; ABV88459; ABV88459; Spea_3143.
DR   KEGG; spl:Spea_3143; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   Proteomes; UP000002608; 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   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..859
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334819"
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;  97391 MW;  BE2D4C6317A1466E CRC64;
     MQEQYTPSEI EAKVQQHWQD TKTFEVTEDE NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRYQRLQG KNVLQPIGWD SFGLPAENAA IKNNTAPAPW TYENIDYMKN QLKMLGFGYD
     WSREIATCTP EYYRWEQWFF TKLYEKGLVY KKTSSVNWCP NDETVLANEQ VIDGCCWRCD
     TTVEQKEIPQ WFIKITEYAE ELLNDIDTLE EWPEQVKTMQ RNWIGRSEGI EMTFQVAGSD
     QSFDIYTTRP DTVMGVTYVA IAAGHPLAEQ AAINNPALVE FIEECKNADT TEAAMAAMEK
     KGVATGLNAI HPITGKEVPI WVGNFVLMNY GTGAVMSVPA HDQRDYEFAK KYGLNIEAVI
     KPVDGEVDIS EEAYTEKGVL FNSAEFDGLD FQAAFDAIDA KLTAEGKGKR QVNFRLRDWG
     VSRQRYWGAP IPMVTLADGT VMPTPEDQLP VILPEDVVMD GIQSPIKSDK EWAKTTINGQ
     EAFRETDTFD TFMESSWYYA RYCSPHADEM LDPAKANYWL PVDQYIGGIE HACMHLLYFR
     FFHKLLRDTG LVNSNEPAKR LLTQGMVLAD AYYYNNEKGA RVWVAPSDVT VQETDDKGRT
     VKAVDSEGHE LVYTGMSKMS KSKNNGIDPQ EMVDKYGADT VRLFMMFAAP PELTLEWQES
     SVEGAHRFIK RLWKTAHDHI ANGTTAELDV KSLNAAQKEL RRELHKTIAK VGDDIERRQM
     FNTAIASIME LMNRLQKAPS ETDQDKALMQ EALNAVIRLL YPIIPHTCFV LWNELGNQGA
     IEEVLWPEVD ESALVEDSKL IIVQVNGKLR AKITVAADAS KEEVEAAGMA EEGVVKHTED
     KTVRKVIYVP GKLLNIVAN