ID   SYL_SHESH               Reviewed;         863 AA.
AC   A8FZ10;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Ssed_3479;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
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., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP000821; ABV38083.1; -; Genomic_DNA.
DR   RefSeq; WP_012143813.1; NC_009831.1.
DR   AlphaFoldDB; A8FZ10; -.
DR   SMR; A8FZ10; -.
DR   STRING; 425104.Ssed_3479; -.
DR   EnsemblBacteria; ABV38083; ABV38083; Ssed_3479.
DR   KEGG; sse:Ssed_3479; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002015; 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..863
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074844"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           622..626
FT                   /note="'KMSKS' region"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   863 AA;  98073 MW;  FFC1C92C73295E86 CRC64;
     MQEQYKPSEI EAKVQQHWQD KKTFEVTEDE NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VVARYQRLQG KNVLQPIGWD SFGLPAENAA IKNNTAPAPW TYENIDYMKN QLKMLGFGYD
     WSREIATCTP EYYRWEQWFF TKLFEKGLVY KKTASVNWCP NDETVLANEQ VIDGCCWRCD
     TTVEQKEIPQ WFIKITEYAD ELLKDIDQLD EWPEQVKTMQ RNWIGRSEGI EMTFGVVDSE
     ETFDIYTTRP DTVMGVTYVA IAAGHPLAEK AAANNSELSD FIEECKNADT TEAAMAAMEK
     KGVATGLYAT HPLTGKQVPI WAANFVLMNY GTGAVMSVPA HDQRDYEFAT KYGLAIEGVI
     KPSDSDLDIS EEAYTEKGVL FNSGDSFPEL DGLDFQDAFD AIDAKLSSEG KGKRQVNFRL
     RDWGVSRQRY WGAPIPMVTL ADGTVVPTPE DQLPVILPED VVMDGIQSPI KADKEWAKTQ
     INGQEAFRET DTFDTFMESS WYYARYCSPH ADEMLDPAKA NYWLPVDQYI GGIEHACMHL
     LYFRFFHKLL RDIGLVNSDE PAKRLLTQGM VLADAFYYNN EKGARVWVAP SDVTVQETDE
     KGRIQKAVDS EGHELVYTGM SKMSKSKNNG IDPQVMVDKY GADTVRLFMM FAAPPELTLE
     WQESSVEGAH RFIKRLWKVA HDHVAKGATA PLDVKTLDTK QKELRRELHK TIVKVGDDIE
     RRQMFNTAIA SVMELMNRLQ KAPTETQQDR ALMQEALSAV VRLLYPIIPH TSFSLWNDLG
     NEENIEDVRW PEADQSALVE DSKLIIVQVN GKLRAKITVP ADATKEVVEE QGFAEEGVIK
     HTEGKTVRKV IYVPGKLLNI VAN