SYL_STRMU
ID SYL_STRMU Reviewed; 833 AA.
AC Q8DS85;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=SMU_1943;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59553.1; -; Genomic_DNA.
DR RefSeq; NP_722247.1; NC_004350.2.
DR RefSeq; WP_002263843.1; NC_004350.2.
DR AlphaFoldDB; Q8DS85; -.
DR SMR; Q8DS85; -.
DR STRING; 210007.SMU_1943; -.
DR PRIDE; Q8DS85; -.
DR EnsemblBacteria; AAN59553; AAN59553; SMU_1943.
DR KEGG; smu:SMU_1943; -.
DR PATRIC; fig|210007.7.peg.1728; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR PhylomeDB; Q8DS85; -.
DR Proteomes; UP000002512; 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; 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_0000152094"
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; 94410 MW; 257411C9E4D114C1 CRC64;
MVYYNHKAIE NKWQKFWEDN HTFKTGTASS KPKFYALDMF PYPSGAGLHV GHPEGYTATD
ILSRFKRAQG YNVLHPMGWD AFGLPAEQYA MDTGHDPADF TAQNIATFKR QIKSLGFSYD
WDREINTTDP NYYKWTQWIF TKLYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
GYPVVRKPMR QWMLKITAYA ERLLEDLEDL DWPESIKDMQ RNWIGKSTGA NVTFKVKDTD
EEFTVFTTRP DTLFGATYAV LAPEHDLVDI ITTAGQAQAV ADYKHQASLK SDLARTDLAK
EKTGVWTGAY AINPVNGKEI PIWIADYVLA SYGTGAIMAV PAHDERDWEF AKQFNLDIIP
VLEGGNVAEA AYTDDGLHIN SGFLNGLDKA AAIDKMVTWL ETEGVGNKKV TYRLRDWLFS
RQRYWGEPIP IIHWEDGTST ALPENELPLV LPVTKDIKPS GTGESPLANL TDWLEVTRED
GVKGRRETNT MPQWAGSSWY FLRYIDPHND QKLADEDLLK QWLPVDVYVG GAEHAVLHLL
YARFWHKFLY DLGVVPTKEP FQKLFNQGMI LGTSYRDHRG ALVATDKVEK RDGSFFNIET
DEELEQAPAK MSKSLKNVVN PDDVVEQYGA DTLRVYEMFM GPLDASIAWS EEGLEGSRKF
LDRVYRLITT KEIAAKNNGH LDKVYNEVVK TVTEHLEAMR FNTAISQLMI FVNAANKEEQ
LFLDYAKGFI QLLAPFAPHL AEELWQFLTQ SGQSITYVAW PSYDESKLVE DEIEIVLQIK
GKVRAKVVVS KDSSREDLEK IALANDKIQA EVAGKDIVKV IAVPNKLVNI VIK