SYL_YERPS
ID SYL_YERPS Reviewed; 860 AA.
AC Q66DE3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=YPTB1103;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH20343.1; -; Genomic_DNA.
DR RefSeq; WP_002210333.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66DE3; -.
DR SMR; Q66DE3; -.
DR EnsemblBacteria; CAH20343; CAH20343; YPTB1103.
DR GeneID; 66842473; -.
DR KEGG; ypo:BZ17_1440; -.
DR KEGG; yps:YPTB1103; -.
DR PATRIC; fig|273123.14.peg.1524; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000001011; 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; 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; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 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.
FT CHAIN 1..860
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152125"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 619..623
FT /note="'KMSKS' region"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 860 AA; 97051 MW; 34DA41D2A01FD153 CRC64;
MQEQYRPEDI ETQVQLHWQE KQTFKVTEDA SKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
VISRYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNIEYMKN QLKLLGFGYD
WDREIATCKP DYYRWEQWFF TKLYEKGMVY KKTSAVNWCP HDLTVLANEQ VIDGCCWRCD
TKVERKEIPQ WFIKITDYAE QLLNDLDTLE SWPEQVKTMQ RNWIGRSEGV DIVFDVVDSE
EKLSVYTTRP DTFMGVTYVA VAAGHPLSLQ AAATNPALAD FVAECRNTKV AEAEMATMEK
KGMATGLYAI HPLTGEKLPI WAANFVLMDY GTGAVMAVPG HDARDWEFAT KYNLPIKPVI
LAADGSEPDL SQEAMTEKGT LFNSGEFDGL NHEDGFNAIA DKLVALGVGQ RKVNYRLRDW
GVSRQRYWGA PIPMVTLEDG TVVPTPEDQL PVILPEDVVM DGISSPIKAD PEWAKTTVNG
IPGLRETDTF DTFMESSWYY ARYTCPQYDD GMLDPAAANY WLPVDQYVGG IEHAIMHLMY
FRFFHKLLRD AGLVDSDEPA KRLLCQGMVL ADAFYYTGNN GERIWVSPVD AIVERDDKGR
IVKAVDAEGH ELVYAGMSKM SKSKNNGIDP QVMVEKYGAD TVRLFMMFAS PAEMTLEWQE
SGVEGANRFL KRVWRLAFDH TAKGAVKPLD IASLTEEQKS LRRDLHKTIA KVTDDVGRRQ
TFNTAIAAVM ELMNKLGRAP QETEQDRALM QEALLAVVRM LYPFTPHVCF SLWQALGGEG
DIDTAPWPIA DEQAMVEDSK LVVVQVNGKV RGRITVPADA TEQQVRERAG QEHLVAKYLD
GVTVRKVIYV PGKLLNLVVG