SYL_TROWT
ID SYL_TROWT Reviewed; 806 AA.
AC Q83GC6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=TWT_385;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
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; AE014184; AAO44482.1; -; Genomic_DNA.
DR RefSeq; WP_011102542.1; NC_004572.3.
DR AlphaFoldDB; Q83GC6; -.
DR SMR; Q83GC6; -.
DR STRING; 203267.TWT_385; -.
DR PRIDE; Q83GC6; -.
DR EnsemblBacteria; AAO44482; AAO44482; TWT_385.
DR KEGG; twh:TWT_385; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; DIDWADV; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002200; 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; Reference proteome.
FT CHAIN 1..806
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152111"
FT MOTIF 54..64
FT /note="'HIGH' region"
FT MOTIF 571..575
FT /note="'KMSKS' region"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 806 AA; 92300 MW; 6A6153B7178A397B CRC64;
MHALRALDTL CENMEYNFRA LEEKWAPIWE RDRLFEVDEN DSETPRKYVL DMFSYPSGDL
HMGHAETYAY GDFIARYWRH RGYNVLHPVG WDSFGLPAEN AAIKHGSDPK VWTYRNIDQQ
ARSMRLYAAS FDWSRRLHTS DPEYYRWNQW LFLKLYKHGL AYRKKAWVNW DPSDRTVLAN
EQVLPDGTSE RSGALVVKKK LTQWFLRITA YADRLLDDLS MLENNWPERV ITMQRNWIGR
SEGVSIEFNI PTLKRPVTVF TTRPETIFGV TYLALAFDSE VTEELASKSG VLGELLELRH
NIDKTHEGVR GLDLKSFAIH PLTGQSVPIF AASYILSDYA KGAVMSVPGH DTRDERFAVR
YNLPIVKIME DNRLISSGKY SGQSVTQARE NITRDLCAKS LGRREISYRL RDWLISRQRY
WGTPIPILYD SNGSEIPVEE DDLPVLLPDS EGIDLTPSGL SPLGGIHDWV NLHKAGSLFR
RDTDTMDTFF DSSWYFLRYL NPDCDTAPFT LEKAKKWGPV DQYCGGVEHA VLHLLYARFI
TKFLYDIGFV DFKEPFLRLI NQGMVVLNGA KMSKSKGNIV EFSKEVSQHG VDVIRFALIF
SGPPEEDIDW KDVSMTGAAR FLSRCIQTAK EVPKRTADLS LGDIELRKHT HSLLNDIDWL
VDSYRFNVIA ARLMDLLNIT RKKIQTIGAD NPAIREAIET IAIALDMFSP YTAEEMWEIL
GNKYSVSKAL FPEVDTTFLE QKTTCAIVQI DGRLRGRLNV LTNITTEQLV HSARSLPAIE
HALSGRSVKR VICVPPKLVN FVVEPK
