ID   SYL_ARTS2               Reviewed;         843 AA.
AC   A0JX57;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Arth_2247;
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB24;
RX   PubMed=24501649; DOI=10.4056/sigs.4438185;
RA   Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA   Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT   "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL   Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK03627.1; -; Genomic_DNA.
DR   RefSeq; WP_011692091.1; NC_008541.1.
DR   AlphaFoldDB; A0JX57; -.
DR   SMR; A0JX57; -.
DR   STRING; 290399.Arth_2247; -.
DR   EnsemblBacteria; ABK03627; ABK03627; Arth_2247.
DR   KEGG; art:Arth_2247; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; DIDWADV; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000754; 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..843
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334729"
FT   MOTIF           61..71
FT                   /note="'HIGH' region"
FT   MOTIF           606..610
FT                   /note="'KMSKS' region"
FT   BINDING         609
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   843 AA;  92600 MW;  9C5CE6DF8B5BFEB1 CRC64;
     MSVQPETETG TAAVATEGPE EGTYSFAAME AKWPQVWEDL KVFTPVDDGS RERRYVLDMF
     PYPSGDLHMG HAEAFAMGDV VARYLRQKGY DVLHPIGWDS FGLPAENAAI KRNAHPSEWT
     YANIDTQAAS FKRYAISADW SRRLHTSDPE YYRWTQWLFK RFYERGLAYR KDSPVNWCPK
     DQTVLANEQV VNGACERCGT AVTKKSLNQW YFKITDYADR LLDDMDELRG HWPERVLAMQ
     KNWIGRSEGA HVNFVIEAAG DKPAKDVTVF TTRPDTLYGA TFFVVAADAP MAVELVTDEH
     AAALDAYREQ VKALSEIERQ STEREKTGVF TGRYAVNPLN GEKLPVWAAD YVLADYGTGA
     IMAVPAHDQR DLDFARTFDL PVRAVLDTGE DDPAVTGKAT AGEGTLINSG VLDGLPKAEA
     IPTAIDMLEK QGTGEKFVNF RLRDWLLSRQ RFWGTPIPII HCPACGEVPV PDDQLPVTLP
     ADLRGEDLSP KGTSPLAAAE AWVNVECPNC HGPAKRDTDT MDTFVDSSWY FLRFVSPQYT
     EGPFDPKKIN DWMPVGQYVG GVEHAILHLL YARFFTKVIH DLGMIDADEP FSALLNQGQV
     LNGGKAMSKS LGNGVDLGEQ LDKYGVDAVR LTMIFASPPE DDVDWADVSP SGSAKFLARA
     WRLAQDVSSA PGADAAQGDR ALRSVTHRTI ADAAALLDSN KFNVVVAKLM ELVNATRKTI
     DAASGAGGAD PAVREAAEAV AVILSLFAPY TAEDMWNVLG HPASVANAGW PSHDEALLVQ
     DTVTAVVQVQ GKVRDRLEVS PEIGEDELRE LALASENVQR ALDGRGIRTV IVRAPKLVNI
     VPA