ID   SYL_PECAS               Reviewed;         860 AA.
AC   Q6D7L6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, 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=ECA1309;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(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; BX950851; CAG74219.1; -; Genomic_DNA.
DR   RefSeq; WP_011092895.1; NC_004547.2.
DR   AlphaFoldDB; Q6D7L6; -.
DR   SMR; Q6D7L6; -.
DR   STRING; 218491.ECA1309; -.
DR   EnsemblBacteria; CAG74219; CAG74219; ECA1309.
DR   KEGG; eca:ECA1309; -.
DR   PATRIC; fig|218491.5.peg.1335; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000007966; 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; Reference proteome.
FT   CHAIN           1..860
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152016"
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;  97095 MW;  E2B24E22728C2512 CRC64;
     MQEQYRPEEI EADVQLHWQE KQTFKVTEQL GKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
     VISRYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYANIDYMKN QLKLLGFGYD
     WDREIATCKP DYYRWEQWFF TKLYEKGLVY KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD
     TKVERKEIPQ WFIKITAYAD QLLNDLDTLE SWPEQVKTMQ RNWIGRSEGV EITFDVADSE
     EKLSVYTTRP DTFMGVTYVA VAAGHPLAAQ AAVTNPALAD FIAECRNTKV AEADMATMEK
     KGMATGLYAI HPLNGEKVAI WVANFVLMEY GTGAVMAVPG HDQRDWEFAT KYDLSIKPVI
     LNADGSEPDL SAQAMTEKGS LFNSGEFDGL DFEAGFNAIA DKLVEKGIGE RKVNYRLRDW
     GVSRQRYWGA PIPMMTLEDG TVIPTPEDQL PVILPEDVVM DGITSPLKSN PEWAKTTVNG
     QPALRETDTF DTFMESSWYY ARYTCPQYDQ GMLDPAAANY WLPVDQYVGG IEHAIMHLMY
     FRFFHKLMRD AGLVTSDEPA KRLLCQGMVL ADAFYYLGNN GERIWVSPTD VTVERDEKGR
     IVKATDNEGR DVVYAGMSKM SKSKNNGIDP QIMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGANRFL KRVWRQAFEH TGKGAVTALD ITTLTEDQKS LRRDLHKTIA KVTDDIGRRQ
     TFNTAIAAIM ELMNKLAKAP QESDQDRALT QETLLAVVRM LYPFTPHVCF TLWQALQGEG
     DVDTAPWPVA DENAMVEDSK LVVVQVNGKV RGKITVAADA SEEQVRERAA QEPLVAKYLD
     GVTVRKVIYV PGKLLNLVVG