ID   SYL_MANSM               Reviewed;         860 AA.
AC   Q65VR5;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=MS0338;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(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; AE016827; AAU36945.1; -; Genomic_DNA.
DR   RefSeq; WP_011199520.1; NC_006300.1.
DR   AlphaFoldDB; Q65VR5; -.
DR   SMR; Q65VR5; -.
DR   STRING; 221988.MS0338; -.
DR   EnsemblBacteria; AAU36945; AAU36945; MS0338.
DR   KEGG; msu:MS0338; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000607; 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_0000152040"
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;  97814 MW;  A5D49243B05C04C4 CRC64;
     MQEQYRPDLL EQEVQKYWQN NQTFKAVKDS SKEKYYCLSM FPYPSGRLHM GHVRNYTIAD
     VVSRYQRMNG KNVLQPVGWD AFGLPAEGAA VKNKTAPAKW TYENIDYMKN QLKMLGFSYD
     WDREIATCKP EYYKWEQWFF TELYKKGLVY KKTSVVNWCP NDETVLANEQ VHEGCCWRCD
     TPVEQKEIPQ WFIKITDYAE QLLSGLDTLP EWPDMVKTMQ RNWIGRSEGV EITFKIENSD
     ETVAVYTTRP DTFYGVSYMA VAAGHPLAEK AAQNNAELAR FIQECKNTKV AEAELATMEK
     KGMATGINAI HPITGKPVPV WVANFVLMHY GTGAVMAVPA HDQRDFEFAT KYGLPIKQVI
     APMNGEEIDL TKAAFTEHGK LVNSAEFDGL DFEAAFNGIA DKLEKMGVGK RQVNYRLRDW
     GVSRQRYWGA PIPMLTLENG DVVPAPLQDL PIVLPEDVVM DGVKSPIKAD PDWAKTSYNG
     QPALKETDTF DTFMESSWYY ARYTSPQYHE GMLDSDEANY WLPVDQYIGG IEHATMHLLY
     FRFFHKLLRD AGLVSTDEPT KKLLCQGMVL ADAFYYTSPT NERIWVSPTK VMLERDEKGR
     ILKATDDEGH ELVHAGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGAKRFL GRLWNLVFEY NKNPVKTAPN PTALSSAQKA LRRDVHKTIA KVSDDIGRRQ
     TFNTAIAAIM ELMNKLTRAP LTDEQDRAVM GEALSAVVRM LYPITPHICF QLWKDLGNED
     IIDFAPWVQA DEAAMIDDEK LVVVQVNGKV RGKITVPADM AEEEIKRVAL AEENVQKFLD
     GLNIVKVIYV PGKLLSFVAK