SYL_CHLTR
ID SYL_CHLTR Reviewed; 819 AA.
AC O84211;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=CT_209;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67801.1; -; Genomic_DNA.
DR PIR; C71544; C71544.
DR RefSeq; NP_219713.1; NC_000117.1.
DR RefSeq; WP_010725124.1; NC_000117.1.
DR AlphaFoldDB; O84211; -.
DR SMR; O84211; -.
DR STRING; 813.O172_01130; -.
DR EnsemblBacteria; AAC67801; AAC67801; CT_209.
DR GeneID; 884917; -.
DR KEGG; ctr:CT_209; -.
DR PATRIC; fig|272561.5.peg.224; -.
DR HOGENOM; CLU_004427_0_0_0; -.
DR InParanoid; O84211; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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..819
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152000"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 600..604
FT /note="'KMSKS' region"
FT BINDING 603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 819 AA; 92903 MW; 82412A659AFAFECF CRC64;
MRYDPGLIEE KWQKFWENEQ VFKAEEDETK TKYYVLDMFP YPSGAGLHVG HLIGYTATDI
VARYKRAQGF SVLHPMGWDS FGLPAEQYAI RTGTHPRETT EKNIANFKKQ LTAMGFSYDE
SREFATSDPE YYKWTQKLFL ILYEKGLAYM ADMAVNYCPE LGTVLSNEEI ENGFSVDGGY
PVERRMLRQW VLRITAFADQ LLEGLDELDW PESVKQLQKN WIGKSSGASV NFATEHGVIE
VFTTRPDTLI GVSFLALAPE HPLVDLLTSD EQKAVVAQYI KETQSKSERD RISEMKTKSG
VFTGSYAKHP VTHKLIPIWI ADYVLIGFGS GAVMGVPAHD ERDLLFAEQF NLPVVSVLNK
EGVCINSCCE GFHLDGLSGE EAKQYVINFL EENHLGAAKI AYKLRDWLFS RQRYWGEPIP
IIHFEDGSCR PLRDYELPLL PPEIQDYRPE GVGQGPLAKV REWVQVFDTE TQRAGKRETH
TMPQWAGSCW YYLRFCDAHN SAAPWAKEKE QYWMPVDLYI GGAEHAVLHL LYARFWHQVF
YEAGIVSTPE PFKKLVNQGL VLATSYRIPG KGYIYPEIAK EENGKWVAPS GEELDVRQEK
MSKSKLNGVD PQILIDEFGA DAVRMYAMFS GPLDKNKLWS NQGVAGCRRF LNRFYEMVSS
DRVKEDNNFE GLSLAHKLVQ RVTDAIEKLS LNTIPSSFME FINDFVKLAV YPKSAVEMAV
RALAPIAPHI SEELWVLLGN SPGVQKSGWP SVLPEYLEGQ TVTIVVQVNG KLRARLDIMK
DASKEEVLAL ARESASKYLE GCEVKKAIFV PARLVNFVV
