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SYL_ENTFA
ID   SYL_ENTFA               Reviewed;         804 AA.
AC   Q837N5;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=EF_0801;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(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; AE016830; AAO80614.1; -; Genomic_DNA.
DR   RefSeq; NP_814544.1; NC_004668.1.
DR   RefSeq; WP_010706700.1; NZ_KE136527.1.
DR   AlphaFoldDB; Q837N5; -.
DR   SMR; Q837N5; -.
DR   STRING; 226185.EF_0801; -.
DR   EnsemblBacteria; AAO80614; AAO80614; EF_0801.
DR   KEGG; efa:EF0801; -.
DR   PATRIC; fig|226185.45.peg.2737; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001415; 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..804
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152015"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   804 AA;  91839 MW;  C79970F0DDFC14B5 CRC64;
     MSYNHKEIEK KWQKYWAKNN CFNTLDDPNK EKFYALDMFP YPSGQGLHVG HPEGYTATDI
     LSRMKRAQGY NVLHPMGWDA FGLPAEQYAL DTGNDPAEFT KKNIETFRRQ INSLGFSYDW
     NREINTTDPE YYKWTQWIFT KLYEKGLAYE AEVAVNWVPE LGTVISNEEV IDGKSERGGY
     DVVRRPMRQW MLKITAYADR LLEDLELVDW PESIKDMQRN WIGRSEGANV TFKVAGTEES
     FTVFTTRPDT LFGATYTVLA PELELVKKIT TPEQTAAVEA YIEETSKKSD LNRTDLAKEK
     TGVFTGAYAI NPVNGQEIPI WIGDYVLASY GTGAIMAVPA HDERDYEFAK TFGIDILPVI
     AGGDITTEAY TGDGPHINSD FLNGLNKAEA IAKMNEWLEE NHVGKKEVSY RLRDWLFSRQ
     RYWGEPIPVI HWEDGTTTTV PESELPLRLP VTSDIRPSGT GESPLANIDE WVNVVDPETG
     MKGKRETNTM PQWAGSSWYY LRFIDPHNKN EIADFEKLKR WLPVDIYIGG AEHAVLHLLY
     ARFWHKFLYD IGVVPTKEPF QKLYNQGMIL GENNEKMSKS RGNVVNPDDV VAKYGADTLR
     LYEMFMGPLD ASIAWNENGL EGSRKFLDRV WRLIVDEEGK MRDRITTIND GRLTKVYHQT
     VKKVTEDMAN LHFNTAISQL MVFVNEANKV DALPYEYVEG FVQLLAPIAP HIGEELWQIL
     GNEESLTYVP WPTYDETALV EDEVEVVFQV NGKLRGKQNV ARGLSKEELE QIAMNHEAVK
     EFIEGKTVRK VIAVPDKLVN IVAN
 
 
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