SYL_BURTA
ID SYL_BURTA Reviewed; 864 AA.
AC Q2SZ91;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=BTH_I1211;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABC38901.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000086; ABC38901.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_025369769.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SZ91; -.
DR SMR; Q2SZ91; -.
DR PRIDE; Q2SZ91; -.
DR EnsemblBacteria; ABC38901; ABC38901; BTH_I1211.
DR KEGG; bte:BTH_I1211; -.
DR HOGENOM; CLU_004427_0_0_4; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001930; Chromosome I.
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.
FT CHAIN 1..864
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334737"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 624..628
FT /note="'KMSKS' region"
FT BINDING 627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 864 AA; 96200 MW; 258DD36105B206A7 CRC64;
MHERYVPADV EAAAQSDWRA ADAYRSKEDA NRKKFYCVSM LPYPSGKLHM GHVRNYTIND
VMYRYLRMNG YNTLMPMGWD AFGMPAENAA MANGVPPAQW TYDNIAYMKK QMQSMGLAID
WSREVTTCKP DYYKWNQWLF LKMLEKGIAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG
ALVEKREIPM YYMRITQYAD ELLNDLDGLG WPERVKIMQQ NWIGKSFGVN FGFPYELDGE
KKLLRVFTTR ADTIMGVTFC AIAAEHPLAA RLAQDKPELQ AFIDECKRGG VAEADIATME
KKGVATGFSV SHPLTGAPVE VWIGNYVLMS YGEGAVMGVP AHDERDFAFA KKYGLPIRQV
IAVEGETYST DAWQEWYGDK TRAVCVNSGK YDGLAYDAAV DAIAADLKAG GFGDKQITYR
LRDWGISRQR YWGTPIPIIH CPSCGDVPVP EQDLPVVLPE DLVPDGTGNP LAKSDAFLNC
ACPKCGAAAK RETDTMDTFV DSAWYFSRYA APDAQTMVDA RTDYWMPMDQ YIGGIEHAIL
HLLYSRFWAK VMRDLGLVAF GEPAKNLLTQ GMVLNETFYR EDAAGKKTWY NPADVTVSFD
DKGRPVGAVL KADGQPVVLG GIEKMSKSKN NGVDPQMLID HYGADTARLF TMFAAPPEQQ
LEWSGAGVDG ASRFLRRVWA FGFANREALA VRAPFDVAQL AEADKTLRRE IHGVLKQADF
DYQRLQYNTV VSAAMKMLNA IEGAKGATPA VLRETYGVLL RVLYPVVPHV TYELWKALGY
ADEFGPLLDA PWPKVDEAAL EQAEIELVLQ INGKVRGALK VAKDASREAI EAAAVADEMF
AKFAEGKPAK KIIVVPGRLV NVVV
