ID   SYL_PAEAT               Reviewed;         842 AA.
AC   A1R6X5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 117.
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=AAur_2246;
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX   NCBI_TaxID=290340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1;
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA   Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT   aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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=ABM09960.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000474; ABM09960.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043806115.1; NC_008711.1.
DR   AlphaFoldDB; A1R6X5; -.
DR   SMR; A1R6X5; -.
DR   STRING; 290340.AAur_2246; -.
DR   PRIDE; A1R6X5; -.
DR   EnsemblBacteria; ABM09960; ABM09960; AAur_2246.
DR   KEGG; aau:AAur_2246; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000637; 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   Gene3D; 3.90.740.10; -; 1.
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   PANTHER; PTHR43740; PTHR43740; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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..842
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334728"
FT   REGION          390..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           62..72
FT                   /note="'HIGH' region"
FT   MOTIF           607..611
FT                   /note="'KMSKS' region"
FT   BINDING         610
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   842 AA;  93067 MW;  FF6EE5D4F0C75C80 CRC64;
     MSVKPETETG TAQTAAAEAP EEGVYSFAAM EAKWPQVWED LKVFTPADDG SRERRYVLDM
     FPYPSGDLHM GHAEAFAMGD VVARYLRQKG FDVLHPIGWD SFGLPAENAA IKRNAHPSEW
     TYANIDTQAA SFKRYAISAD WSRRLHTSDP EYYRWTQWLF KRFYERGLAY RKDSPVNWCP
     KDLTVLANEQ VVNGACERCG TPVTKKSLNQ WYFKITDYAD RLLEDMDQLQ GHWPERVLAM
     QRNWIGRSEG AHVRFVIEAT ADRAEREVTV FTTRPDTLYG ATFFVVAADA HLALDLVTPE
     QHDELMAYRE KVKALSEIER QSTEREKTGV FTGRYAINPL NGEKLPVWAA DYVLADYGTG
     AIMAVPAHDQ RDLDFAKTFG LPVRAVLDTG DEDPAETGVA TAGEGTLKNS GELDGLSKSE
     GIPAAIEILE KLGTGEKFVN FRLRDWLLSR QRFWGTPIPI IHCGECGEVP VPDDQLPVRL
     PDDLRGEALS PKGTSPLAAA VEWVNVECPN CGRAAQRDTD TMDTFVDSSW YFLRFVSPDY
     TEGPFDPEKI NNWMPVGQYV GGVEHAILHL LYARFFTKVI KDIGLIEANE PFSALLNQGQ
     VLNGGKAMSK SLGNGVDLGE QLDKFGVDAV RLTMVFASPP EDDVDWADVS PSGSAKFLAR
     AWRLGQDVSS EPGVDPATGD RALRTVTHKT IADAAELLDN NKFNVVVARL MELVNATRKT
     IDSGAGAADP AVREAVEAVA VILSLFAPYT AEDLWNTLGH PASVANAGWP KHDDALLVQD
     TVTAVVQVQG KVRDRLEVSP DITEDALREL ALASENVQRA LDGRGIRTVI VRAPKLVNIV
     PA