ID   SYL_JANMA               Reviewed;         881 AA.
AC   A6T239;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=mma_2896;
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille;
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA   Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the convergent
RT   evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR89205.1; -; Genomic_DNA.
DR   RefSeq; WP_012080745.1; NC_009659.1.
DR   AlphaFoldDB; A6T239; -.
DR   SMR; A6T239; -.
DR   STRING; 375286.mma_2896; -.
DR   EnsemblBacteria; ABR89205; ABR89205; mma_2896.
DR   KEGG; mms:mma_2896; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; JSP375286:MMA_RS15025-MON; -.
DR   Proteomes; UP000006388; 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; 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; 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..881
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009354"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   881 AA;  98999 MW;  0B6DE8EE81B226D6 CRC64;
     MQDKYSPAEV EKSAHDHWQA IDAYKAVENA KDKNGKDKKK FYACSMLPYP SGKLHMGHVR
     NYTINDVMYR YLRMNGYNVL MPMGWDAFGM PAENAAMANN VPPAQWTYAN IDYMKTQMAS
     MGLAIDWSRE MTACRPEYYK WNQWMFLKML EKGIIYKKTG TVNWDPIDQT VLANEQVIDG
     RGWRSGALIE KREIPMYYAR ITDYAEELLD HVDNKLPGWP ERVRIMQSNW IGKSTGVRFA
     FTHDIAEEGK LINDGKLWVF TTRADTIKGV TFCAVAPEHA LATFAAKSNP ELTDFIAECK
     LGSVIEADMA TMEKKGMPTG LFVKHPLTGQ LVEVWVGNYV LITYGDGAVM GVPAHDERDF
     AFAQKYVLPI HPVIDVPGKT FSDVAWHEWY GDKENGRCIN SGKYDGLNYQ QAVDAIAADL
     AELGLGEKKI TYRLRDWGIS RQRYWGTPIP IIHCKDCGDV PVPEKDLPVV LPEDCVPDGS
     GNPLNKHEKF LHVDCPQCGK PARRETDTMD TFVDSSWYYM RYCSPNSSDA MVDSRNDYWM
     PMDQYIGGIE HAVLHLLYAR FWTKVMRDFG LVKFDEPFTN LLTQGMVLNE TYFREDASGK
     KTWFNPADVQ LQLDDKGRPV SAVLSSDGKA VEIGGTEKMS KSKNNGIDPQ AQIDQYGADT
     ARLFTMFASP PEQTLEWSGA GVEGANRFLR RVWAYGYNQA ARVANASAFD FATLPEAHKA
     LRRETHKILQ QADNDYKRIQ YNTVVSASMK MLNTLEAAKL DDSPASNAVI SEGLSIFLRI
     LNPVAPHITH ALWQELGFAK DHGDILDAPW PQVDPAALEQ AEIEMMIQVN GKLRGSIIVA
     KDADKASIEA AALANESVQK FIEGTPKKII VVPGKLVNIV A