ID   SYL_CHLP8               Reviewed;         807 AA.
AC   B3QM08;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, 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}; OrderedLocusNames=Cpar_0539;
OS   Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS   subsp. thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 263 / NCIMB 8327;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-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; CP001099; ACF10961.1; -; Genomic_DNA.
DR   RefSeq; WP_012501794.1; NC_011027.1.
DR   AlphaFoldDB; B3QM08; -.
DR   SMR; B3QM08; -.
DR   STRING; 517417.Cpar_0539; -.
DR   PRIDE; B3QM08; -.
DR   EnsemblBacteria; ACF10961; ACF10961; Cpar_0539.
DR   KEGG; cpc:Cpar_0539; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008811; 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; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..807
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091303"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   807 AA;  92556 MW;  D495F8BEC478107D CRC64;
     MKYDFSALEK KWQARWADEQ TFASSADQDK PKYYVLDMFP YPSGSGLHVG HLEGYTATDI
     MARYKRCQGH NVLHPMGWDA FGLPAEQFAI KTGTHPRLTT EKNVASFRET LKSMGFSYDW
     SREVNTTDPN YFKWTQWIFL KLYEKGLAYI SEVDVNWCEE LKVVLANEEV DEKIADGYTV
     VRRPLRQWVL KITAYAERLL EDLDEVDWPE NVKQMQRNWI GRSEGVEIDF ELRCHRTNLR
     VYTTRPDTLF GATYLVISPE HPMAEKLAIA QQLVEVKKYI EQAKLKTELE RTGLQKEKTG
     VFTGSYAINP ANGEALPVWI SDFVLTSYGT GAIMSVPAHD SRDWEFAKKF GLPIREVIKS
     PHDVQEEVFD GKESVCVNSA NDEISIDGLD FKTAFDRMAT WLESKGKGKR KVNYKLRDWV
     FSRQRYWGEP IPIKHYEDGT MRPETNLPLT LPEVEAYHPT STGESPLANI ESWLYGEDEH
     GKFRRETNTM PQWAGSCWYY LRFIDPQNGN ALVDPSREQY WMNVDLYIGG AEHAVLHLLY
     SRFWHKVLYD LGVVSTKEPF QRLFNQGMIL GEDNEKMSKS RGNVIPADHV LSTYGADAVR
     LYEMFLGPLE QVKPWNTHGI EGISRFLNKV WRLVWDENTE TQKTTDDKPS EAVLKRMHKA
     IKKVTEDTEQ LKFNTAISEM MVLVNELTKT GCYSRETTET LLVLLSPFAP HITEELWQTL
     GHTESISGAV WPVFDAKLAT DDVLTIAVQV NGKLRGTFEA PAGYAKEDMI ESAKKVESVA
     KFLEGQQIIK EIAVPGKLVN FAVKPQQ