ID   SYL_ACTP2               Reviewed;         861 AA.
AC   A3N0N2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=APL_0872;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73968.1; -; Genomic_DNA.
DR   RefSeq; WP_005601197.1; NC_009053.1.
DR   AlphaFoldDB; A3N0N2; -.
DR   SMR; A3N0N2; -.
DR   STRING; 416269.APL_0872; -.
DR   EnsemblBacteria; ABN73968; ABN73968; APL_0872.
DR   KEGG; apl:APL_0872; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001432; 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; 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..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009286"
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   861 AA;  97751 MW;  3F8A8665AFF303D5 CRC64;
     MQQQYNPSAI EPKVQQFWAE NKVFKAVKDV TKEKYYCLSM LPYPSGKLHM GHVRNYTIGD
     VVSRYQRMIG KNVLQPMGWD AFGLPAEGAA VKNNTAPAKW TYENIEYMKG QLKMLGFSYD
     WDREVTTCRP EYYKWEQWFF TELYKKGLVY KKTSTVNWCP NDATVLANEQ VHEGCCWRCD
     TPVEQREIPQ WFIKITDYAE ELLTHLDNLP QWPDQVKTMQ RNWIGRSEGV EITFKIAGSN
     AELPVYTTRP DTFFGVSYVA IAAAHPLAEM AAENNPALAE FIREAKNTKV AEAELATMEK
     KGMATGLFAI HPLTGKEVPV WVANFVLMHY GTGAVMAVPA HDERDFEFAQ KYGLQINQVI
     QPLDGSEWDF SKAAYTEHGK LINSAEFDDL NFEQAFNAIA DKLESMKVGK RQVNFRLRDW
     GVSRQRYWGA PIPMMTTEDG EVVTVPMQDL PVILPEDVVM NGVQSPIKAD PEWAKTTYNG
     KPALKETDTF DTFMESSWYY ARYTCPQYHE GMLDSDEANY WLPVDQYIGG IEHATMHLLY
     FRFFHKLLRD AGILNSDEPA TKLLCQGMVL ADAFYYTSPT NERIWVSPTQ VTLERDEKGR
     IIKATDPEGR ELVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGAKRFL GRVWNLVYEY SQNPATAALD VAALSKAQKE LRRDVHKTIA KVSDDIGRRQ
     TFNTAIAAIM ELMNKLTKAP LENEQDKAVM AEALSAVVRM LYPITPHICF ELWQALGNND
     TIDFAPWVVA DESAMVEDEK LVVVQVNGKV RGKVTVSATA TEDEVKAIAK ADANVAKFLE
     GVEIVKEIYV PYKMLSFAVK A