ID   SYL_CHLTE               Reviewed;         807 AA.
AC   Q8KBY2;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=CT1650;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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   ---------------------------------------------------------------------------
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; AE006470; AAM72875.1; -; Genomic_DNA.
DR   RefSeq; NP_662533.1; NC_002932.3.
DR   RefSeq; WP_010933314.1; NC_002932.3.
DR   AlphaFoldDB; Q8KBY2; -.
DR   SMR; Q8KBY2; -.
DR   STRING; 194439.CT1650; -.
DR   EnsemblBacteria; AAM72875; AAM72875; CT1650.
DR   KEGG; cte:CT1650; -.
DR   PATRIC; fig|194439.7.peg.1492; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001007; 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; 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; 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; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..807
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151999"
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;  92478 MW;  24F1202D3C5B9205 CRC64;
     MKYDFSALEK KWQSRWADEQ TFASSADQEK PKYYVLDMFP YPSGSGLHVG HLEGYTATDI
     MARYKRCQGH NVLHPMGWDA FGLPAEQFAI KTGTHPRLTT EKNVASFRET LKSMGFSYDW
     SREINTTDPN YFKWTQWIFL KLYEKGLAYI SEVDVNWCEE LKVVLANEEV DEKIADGYTV
     VRRPLRQWVL KITAYAERLL KDLDEVDWPE NVKQMQRNWI GRSEGMEIDF ELRCHRTNLR
     VYTTRPDTLF GATYLVISPE HPMAEKLAIA QQLVAVKKYI EQAKLKTELE RTGLQKEKTG
     VFTGSYAINP ANGEALPVWI SDFVLTSYGT GAIMSVPAHD SRDWEFAKKF GLPIREVIKS
     PHDVQERVFD GKESVCVNSA NDEISINGLD FKTAFDRMAA WLESKGKGKR KVNYKLRDWV
     FSRQRYWGEP IPIKHYEDGT MRPETNLPLT LPEVEAYQPT STGESPLANI ESWLYGEDEH
     GKFRRETNTM PQWAGSCWYY LRFIDPQNSD ALVDPSLEQY WMNVDLYIGG AEHAVLHLLY
     SRFWHKVLYD LGVVSTKEPF QRLFNQGMIL GEDNEKMSKS RGNVIPADHV LSTYGADALR
     LYEMFLGPLD QVKPWNTHGI EGISRFLNKV WRLVWDENTE TQKTTEDKPS EAILKRMHKA
     IKKVTEDTEQ LKFNTAISEM MVLVNELHKA GCYSRETTET LLVLLSPFAP HITEELWQAL
     GHAESISGAV WPVFDAKLAT DDVLTIAVQV NGKLRGTFEA PAGCTKEEMI ESAKKVESVA
     KFLDGQQIVK EIAVPGKLVN FAVKPQQ
//