ID   SYL_SHEHH               Reviewed;         859 AA.
AC   B0TR44;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 81.
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=Shal_3228;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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=ABZ77775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000931; ABZ77775.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041416511.1; NC_010334.1.
DR   AlphaFoldDB; B0TR44; -.
DR   SMR; B0TR44; -.
DR   STRING; 458817.Shal_3228; -.
DR   PRIDE; B0TR44; -.
DR   EnsemblBacteria; ABZ77775; ABZ77775; Shal_3228.
DR   KEGG; shl:Shal_3228; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001317; 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.
FT   CHAIN           1..859
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334818"
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;  97166 MW;  AC6E2982B3F9764E CRC64;
     MQEQYTPSEI EAKVQQHWQD TKTFEVTEDA NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRYQRLQG KNVLQPIGWD SFGLPAENAA IKNSTAPAPW TYENIDYMKN QLKMLGFGYD
     WSREIATCTP EYYRWEQWFF TKLYEKGLVY KKTSSVNWCP NDETVLANEQ VIDGCCWRCD
     TTVEQKEIPQ WFIKITEYAE ELLNDLDQLD EWPEQVKTMQ RNWIGRSEGI EMTFQVADSD
     QSFDIYTTRP DTVMGVTYVA IAAGHPLAEQ AAINNPALAE FIEECKNADT TEAAMAAMEK
     KGVATGLNAI HPITGKEVPI WVGNFVLMNY GTGAVMSVPA HDQRDYEFAK KYSLNIEAVV
     KPADGEVDIS EEAYTEKGVL FNSAEFDGLD FQAAFDAIDA KLTAEGKGKR QVNFRLRDWG
     VSRQRYWGAP IPMVTLADGT VIPTPEDQLP VILPEDVVMD GIQSPIKSDK EWAKTTVNGQ
     EAFRETDTFD TFMESSWYYA RYCSPHADQM LDPAKANYWL PVDQYIGGIE HACMHLLYFR
     FFHKLLRDSG LVNSDEPAKR LLTQGMVLAD AYYYNNEKGA RVWVAPSDVT VLETDDKGRT
     VKAVDSEGNE LVYTGMSKMS KSKNNGIDPQ EMVDKYGADT VRLFMMFAAP PELTLEWQES
     SVEGAHRFIK RLWKTAHDHI ATGPTAELDV KSLNAAQKEL RRELHKTIAK VGDDIERRQM
     FNTAIASVME LMNRLQKAPS ETEQDKALMQ EALNAVVRLL YPIIPHTCFV LWNDLGNQGA
     IEDVLWPEVD ESALVEDSKL IIVQVNGKLR AKITVAADAS KEEVETAGMA EEGVVKHTEG
     KTVRKVIYVP GKLLNIVAN