ID   SYL_SHIB3               Reviewed;         860 AA.
AC   B2TU77;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
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=SbBS512_E0609;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP001063; ACD09066.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2TU77; -.
DR   SMR; B2TU77; -.
DR   STRING; 344609.SbBS512_E0609; -.
DR   KEGG; sbc:SbBS512_E0609; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   Proteomes; UP000001030; 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; Reference proteome.
FT   CHAIN           1..860
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091364"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   860 AA;  97208 MW;  7DB0BDF4F21F8034 CRC64;
     MQEQYRPEEI ESKVQLHWDE KRTFEVTEDE SKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
     VIARYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNIAYMKN QLKMLGFGYD
     WSRELATCTP EYYRWEQKFF TELYKKGLVY KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD
     TKVERKEIPQ WFIKITAYAD ELLNDLDKLD HWPDTVKSMQ RNWIGRSEGV EITFNVNDYD
     NTLTVYTTRP DTFMGCTYLA VAAGHPLAQK AAENNPELAA FIDECRNTKV AEAEMATMEK
     KGVDTGFKAV HPLTGEEIPV WAANFVLMEY GTGAVMAVPG HDQRDYEFAS KYGLNIKPVI
     LAADGSEPDL SQQALTEKGV LFNSGEFNGL DHEAAFNAIA DKLTAMGVGE RKVNYRLRDW
     GVSRQRYWGA PIPMVTLEDG TVMPTPDDQL PVILPEDVVM DGITSPIKAD PEWAKTTVNG
     MPALRETDTF DTFMESSWYY ARYTCPEYKE GMLDSEAANY WLPVDIYIGG IEHAIMHLLY
     FRFFHKLMRD AGMVNSDEPA KQLLCQGMVL ADAFYYVGEN GERNWVSPVD AIVERDEKGR
     IVKAKDAAGH ELVYTGMSKM SKSKNNGIDP QVMVERYGAD TVRLFMMFAS PADMTLEWQE
     SGVEGANRFL KRVWKLVYEH TAKGDVAALN VDGLTEDQKA LRRDVHKTIA KVTDDIGRRQ
     TFNTAIAAIM ELMNKLAKAP TDGEQDRALM QEALLAVVRM LNPFTPHICF TLWQELKGEG
     DIDNAPWPVA DEKAMVEDST LVVVQVNGKV RAKITVPVDA TEEQVRERAG QEHLVAKYLD
     GVTVRKVIYV PGKLLNLVVG
//