ID   SYL_ACTP7               Reviewed;         834 AA.
AC   B3H1L1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=APP7_0931;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001091; ACE61583.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3H1L1; -.
DR   SMR; B3H1L1; -.
DR   EnsemblBacteria; ACE61583; ACE61583; APP7_0931.
DR   KEGG; apa:APP7_0931; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001226; 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.
FT   CHAIN           1..834
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091282"
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   834 AA;  95323 MW;  52784EF8F74B087F CRC64;
     MQQQYNPSAI EPKVQQFWAE NKVFKAVKDV TKEKYYCLSM LPYPSGKLHM GHVRNYTIGD
     VVSRYQRMIG KNVLQPMGWD AFGLPAEGAA VKNNTAPAKW TYENIEYMKG QLKMLGFSYD
     WDREVTTCRQ 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 RVKLPFRQQQ PKMKSKQLRK RMQT