SYL_STAAE
ID SYL_STAAE Reviewed; 805 AA.
AC A6QHU1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=NWMN_1651;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
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; AP009351; BAF67923.1; -; Genomic_DNA.
DR RefSeq; WP_001549041.1; NC_009641.1.
DR AlphaFoldDB; A6QHU1; -.
DR SMR; A6QHU1; -.
DR EnsemblBacteria; BAF67923; BAF67923; NWMN_1651.
DR KEGG; sae:NWMN_1651; -.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000006386; 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; 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; 2.
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.
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..805
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000071113"
FT MOTIF 41..52
FT /note="'HIGH' region"
FT MOTIF 577..581
FT /note="'KMSKS' region"
FT BINDING 580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 805 AA; 91786 MW; CCEF7840099E907F CRC64;
MLNYNHNQIE KKWQDYWDEN KTFKTNDNLG QKKFYALDMF PYPSGAGLHV GHPEGYTATD
IISRYKRMQG YNVLHPMGWD AFGLPAEQYA LDTGNDPREF TKKNIQTFKR QIKELGFSYD
WDREVNTTDP EYYKWTQWIF IQLYNKGLAY VDEVAVNWCP ALGTVLSNEE VIDGVSERGG
HPVYRKPMKQ WVLKITEYAD QLLADLDDLD WPESLKDMQR NWIGRSEGAK VSFDVDNTEG
KVEVFTTRPD TIYGASFLVL SPEHALVNSI TTDEYKEKVK AYQTEASKKS DLERTDLAKD
KSGVFTGAYA TNPLSGEKVQ IWIADYVLST YGTGAIMAVP AHDDRDYEFA KKFDLPIIEV
IEGGNVEEAA YTGEGKHINS GELDGLENEA AITKAIQLLE QKGAGEKKVN YKLRDWLFSR
QRYWGEPIPV IHWEDGTMTT VPEEELPLLL PETDEIKPSG TGESPLANID SFVNVVDEKT
GMKGRRETNT MPQWAGSCWY YLRYIDPKNE NMLADPEKLK HWLPVDLYIG GVEHAVLHLL
YARFWHKVLY DLAIVPTKEP FQKLFNQGMI LGEGNEKMSK SKGNVINPDD IVQSHGADTL
RLYEMFMGPL DAAIAWSEKG LDGSRRFLDR VWRLMVNEDG TLSSKIVTTN NKSLDKVYNQ
TVKKVTEDFE TLGFNTAISQ LMVFINECYK VDEVYKPYIE GFVKMLAPIA PHIGEELWSK
LGHEESITYQ PWPTYDEALL VDDEVEIVVQ VNGKLRAKIK IAKDTSKEEM QEIALSNDNV
KASIEGKDIM KVIAVPQKLV NIVAK