SYL_SALPA
ID SYL_SALPA Reviewed; 860 AA.
AC Q5PM88;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=SPA2086;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(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; CP000026; AAV77980.1; -; Genomic_DNA.
DR RefSeq; WP_001157911.1; NC_006511.1.
DR AlphaFoldDB; Q5PM88; -.
DR SMR; Q5PM88; -.
DR EnsemblBacteria; AAV77980; AAV77980; SPA2086.
DR KEGG; spt:SPA2086; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000008185; 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_1000009422"
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; 96986 MW; 9B1BE5FDECB1F08F CRC64;
MQEQYRPEEI ESKVQLHWDE KRTFEVTEDE SKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
VVARYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNIAYMKN QLKTLGFGYD
WSREIATCTP EYYRWEQKFF TELYKKGLVY KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD
TKVERKEIPQ WFIKITAYAD ELLRDLDKLD HWPDTVKTMQ RNWIGRSEGV EITFDVKGYD
NTLIVYTTRP DTFMGATYLA VAAGHPLAQK AAANNAELAA FVDECRNTKV AEAEMATMEK
KGVDTGYKAI HPLTGEEIPV WAANFVLMEY GTGAVMAVPG HDQRDYEFAS KYGLTIKPVI
LAADGSEPDL SEQALTEKGV LFNSGEFDGL AFEAAFNAIA DKLAEKGVGE RKVNYRLRDW
GVSRQRYWGA PIPMITQEDG TVLPTPEDQL PVILPEDVVM DGITSPIKAD PEWAKTTVNG
MPALRETDTF DTFMESSWYY ARYTCPQYQE GMLDSKAANY WLPVDIYIGG IEHAIMHLLY
FRFFHKLMRD AGMVTSDEPA KQLLCQGMVL ADAFYYVGEN GERNWVSPVD AIVERDEKGR
IVKAKDAAGH ELVYTGMSKM SKSKNNGIDP QVMVERYGAD TVRLFMMFAS PADMTLEWQE
SGVEGANRFI KRVWKLVYEH TAKGPVAALN VDALSEDQKA LRRDVHKTIA KVTDDIGRRQ
TFNTAIAAIM ELMNKLAKAP QEGEQDRALL QEALQAVVRM LNPFTPHVCF TLWQELGGEG
DIDNAPWPVA DEQAMVENTT LVVVQVNGKV RGKITVAVDA TEEQVRERAG QEHLVAKYLD
GVTVRKVIYV PGKLLNLVVG