ID   SYL_PASMU               Reviewed;         860 AA.
AC   P57923;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 135.
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=PM1214;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03298.1; -; Genomic_DNA.
DR   RefSeq; WP_010907077.1; NC_002663.1.
DR   AlphaFoldDB; P57923; -.
DR   SMR; P57923; -.
DR   STRING; 747.DR93_752; -.
DR   PRIDE; P57923; -.
DR   EnsemblBacteria; AAK03298; AAK03298; PM1214.
DR   KEGG; pmu:PM1214; -.
DR   PATRIC; fig|272843.6.peg.1224; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000809; 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..860
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152059"
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;  97623 MW;  30C4308EF6D99E5A CRC64;
     MQEQYRPDLI EAEVQQYWAE NKTFKAIKDT NKPKYYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRYQRMNG KNVLQPMGWD AFGLPAEGAA IKNKTAPAKW TYENIDYMKN QLKILGFGFD
     WDREVTTCKP DYYKWEQWFF TELYKKGLVY KKTSTVNWCP NDETVLANEQ VHEGCCWRCD
     TPVEQKEIPQ WFIKITDYAE QLLGGLDHLP LWPDQVKTMQ RNWIGRSEGV EITFQLANSE
     DNLTVYTTRP DTFFGVSYVA VAAAHPLAEK AAENNPELAQ FIQECKNTKV AEAELATMEK
     KGMATGVYAI HPLTGEKVPV WVANFVLMHY GTGAVMAVPG HDERDAEFAR KYGLPLLNVI
     KPINGEPLLE HELPYCEHGI LFNSGEFNGL DFDAAFNAIA DKLEALGKGK RQVNYRLRDW
     GVSRQRYWGA PIPMLTLENG EVVPAPLQDL PIELPEDVVM DGVKSPIKAD PEWAKTTYNG
     QPALKETDTF DTFMESSWYY ARYTSPKFAE AMLDADEANY WLPVDQYIGG IEHATMHLLY
     FRFFHKLLRD AGFVTSDEPA DKLLCQGMVL ADAFYYTSPT NERIWVSPTE VTLERDEKGR
     ILKAFDKEGR ELVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGAKRFL GRLWNLVFEY NKHPAETTVE PTALSSAQKA LRRDVHKTIA KVSDDIGRRQ
     TFNTAIAAIM ELMNKLTKAP LVEVQDRAIM AEALSAVVRM LYPITPHICF QLWKDLGNTE
     AIDFAPWVEA DAAAMVDDEK LVVVQVNGKV RAKVTVPAEM SEDDIKQVAL ADSNVAKHLE
     GLNIVKTIYV PGKLFSFVAK