SYL_STRP1
ID SYL_STRP1 Reviewed; 833 AA.
AC Q9A1P0; Q491F2;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
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};
GN OrderedLocusNames=SPy_0173, M5005_Spy0147;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(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=AAZ50766.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004092; AAK33273.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ50766.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_268552.1; NC_002737.2.
DR AlphaFoldDB; Q9A1P0; -.
DR SMR; Q9A1P0; -.
DR STRING; 1314.HKU360_00192; -.
DR PaxDb; Q9A1P0; -.
DR EnsemblBacteria; AAK33273; AAK33273; SPy_0173.
DR KEGG; spy:SPy_0173; -.
DR KEGG; spz:M5005_Spy0147; -.
DR PATRIC; fig|160490.10.peg.151; -.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000750; 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 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; Reference proteome.
FT CHAIN 1..833
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152097"
FT MOTIF 41..52
FT /note="'HIGH' region"
FT MOTIF 610..614
FT /note="'KMSKS' region"
FT BINDING 613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
FT CONFLICT 73
FT /note="I -> V (in Ref. 2; AAZ50766)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> S (in Ref. 2; AAZ50766)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="K -> D (in Ref. 2; AAZ50766)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="A -> S (in Ref. 2; AAZ50766)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="N -> K (in Ref. 2; AAZ50766)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="K -> N (in Ref. 2; AAZ50766)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="G -> D (in Ref. 2; AAZ50766)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="K -> N (in Ref. 2; AAZ50766)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 833 AA; 93816 MW; 59168EADE9B9FFB3 CRC64;
MTFYDHTAIE PKWQAFWADN HTFKTGTDAS KPKFYALDMF PYPSGAGLHV GHPEGYTATD
ILSRFKRAQG HNILHPMGWD AFGLPAEQYA MDTGNDPAEF TAENIANFKR QINALGFSYD
WDREVNTTDP NYYKWTQWIF TKLYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
GYPVVRKPMR QWMLKITAYA ERLLEDLEEV DWPESIKDMQ RNWIGKSTGA NVTFKVKDTD
KDFTVFTTRP DTLFGATYAV LAPEHALVDA ITTADQAEAV AKYKRQASLK SDLARTDLAK
EKTGVWTGAY AINPVNGNEM PVWIADYVLA SYGTGAIMAV PAHDERDWEF AKQFKLDIIP
VLEGGNVEEA AFTEDGLHIN SGFLDGLDKA SAIAKMVEWL EAEGVGNEKV TYRLRDWLFS
RQRYWGEPIP IIHWEDGTST AVPESELPLV LPVTKDIRPS GTGESPLANV TDWLEVTRED
GVKGRRETNT MPQWAGSSWY YLRYIDPHNT EKLADEELLK QWLPVDIYVG GAEHAVLHLL
YARFWHKVLY DLGVVPTKEP FQKLFNQGMI LGTSYRDSRG ALVATDKVEK RDGSFFHVET
GEELEQAPAK MSKSLKNVVN PDDVVEQYGA DTLRVYEMFM GPLDASIAWS EEGLEGSRKF
LDRVYRLITT KEITEENSGA LDKVYNETVK AVTEQVDQMK FNTAIAQLMV FVNAANKEDK
LFSDYAKGFV QLIAPFAPHL GEELWQALTA SGESISYVPW PSYDESKLVE NDVEIVVQIK
GKVKAKLVVA KDLSREELQE VALANEKVQA EIAGKDIIKV IAVPNKLVNI VIK
