SYL_STRSV
ID SYL_STRSV Reviewed; 833 AA.
AC A3CKP1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 105.
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=SSA_0289;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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=ABN43746.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000387; ABN43746.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_001034296.1; NC_009009.1.
DR AlphaFoldDB; A3CKP1; -.
DR SMR; A3CKP1; -.
DR STRING; 388919.SSA_0289; -.
DR EnsemblBacteria; ABN43746; ABN43746; SSA_0289.
DR KEGG; ssa:SSA_0289; -.
DR PATRIC; fig|388919.9.peg.279; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002148; 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; 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..833
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334825"
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"
SQ SEQUENCE 833 AA; 94312 MW; 71D6C9940EE2C873 CRC64;
MAYYNHKEIE PKWQKYWAEH HTFKTGTDKD KPNFYALDMF PYPSGAGLHV GHPEGYTATD
ILSRYKRTQG YNVLHPMGWD AFGLPAEQYA MDTGNDPADF TAENIANFKR QINALGFSYD
WDREINTTDP NYYKWTQWIF TKLYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
GYPVVRKPMR QWMLKITAYA ERLLNDLEEL DWPESIKDMQ RNWIGKSTGA NVTFKIKDTD
KDFTVFTTRP DTLFGATYAV LAPEHALVDA ITSAEQAQAV ADYKHAASLK SDLARTDLAK
DKTGVWTGAY AINPVNGKEI PIWIADYVLA SYGTGAIMAV PAHDERDWEF AKQFDLEIIP
VLEGGNVAEA AYTEDGPHIN SGFLDGLDKA AAIDKMVAWL EAEGVGNEKV TYRLRDWLFS
RQRYWGEPIP IIHWEDGTST AVPENELPLV LPVTKDIRPS GTGESPLANL TDWLEVTRED
GVKGRRETNT MPQWAGSSWY YLRYIDPHNN EKLADEELLK AWLPVDIYIG GAEHAVLHLL
YARFWHKFLY DIGVVPTKEP FQKLFNQGMI LGTSYRDSRC ALVATDKVEK RDGSFFNIET
GEELEQAPAK MSKSLKNVVN PDDVVEQYGA DTLRVYEMFM GPLDASIAWS EEGLEGSRKF
LDRVYRLFNS KELVTENSGA LDKVYHETVK SVTEQIEELK FNTAIAQLMI FVNAANKEEK
LYVEYAKGFI QLLAPFAPHL AEELWQAVAQ TGESISYVTW PTYDESKLVE AEVEIVVQIK
GKVRAKLVVA KDLSREELQE IALSDEKIKS EIAGKEIVKV ISVPNKLVNI VVK