ID   SYL_METPP               Reviewed;         897 AA.
AC   A2SC91;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Mpe_A0218;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM93180.1; -; Genomic_DNA.
DR   RefSeq; WP_011827819.1; NC_008825.1.
DR   AlphaFoldDB; A2SC91; -.
DR   SMR; A2SC91; -.
DR   STRING; 420662.Mpe_A0218; -.
DR   PRIDE; A2SC91; -.
DR   EnsemblBacteria; ABM93180; ABM93180; Mpe_A0218.
DR   KEGG; mpt:Mpe_A0218; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000366; 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; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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..897
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334771"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT   MOTIF           654..658
FT                   /note="'KMSKS' region"
FT   BINDING         657
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   897 AA;  98705 MW;  1C9F65043FCFB22D CRC64;
     MSTPHPAPAS AYEPGAIEAA AHAHWTARDA HRVVEDTSRP KFYACSMLPY PSGKLHMGHV
     RNYTINDMMA RYLRMKGYNV LMPMGWDAFG LPAENAAIDK KVAPAQWTRD NIADMKSQMQ
     PLGLAFDWSR EVATCDPDYY KWNQWFFLKL LEKGIAYKKT QVVNWDPVDQ TVLANEQVID
     GRGWRSGAPV ERREIPGYYL AITQYADELL ANVADPASPG FLHGWPERVR LMQEHWIGKS
     AGVRFAFPHE IRDADGTLVG DGLMHVFTTR ADTIMGVTFC AVAPEHPLAT HAAASDPDLA
     AFIETCKAGG TTEAELATKD KEGRPTGLFV KHPLSGAPVP VWVGNYVLMG YGDGAVMGVP
     AHDERDFAFA KKYGIDILQV VHVDGEHFSY DHWQDWYADK QRGVTINSGN LSGLSYPVAV
     DAVAAALAAQ GLGDKKTTWR LRDWGISRQR YWGTPIPIIH CTGSGPGSDN PGCGDVPVPE
     QDLPVLLPED LIPDGSGNPL NKSAAFLNVA CPKCGAPAKR ETDTMDTFVD SSWYYMRYCC
     PDSDAAMVDS RNDYWMPMDQ YIGGIEHAVL HLLYARFWTK AMRDCGLVKF DEPFTKLFTQ
     GMLLNESYYR EDASGKKRWF YPSEVEVQFD DKGHPVGAIA REDGQPVQLG GIEKMSKSKN
     NVVEPRDIIA KFGADTARLF TMFAGPPDQS AAWSDSGAEG SFRYLRRLWA FATKQREAVQ
     AAGTDFADAS RAAIDLRRDV HLLLRQVSHD YDRLQYNTVV SGAMKLLNAL ESAALADTAA
     DRAALREGLG ILLRALYPAA PHIAHALWQD LGYAAAHGDL LDAPWPAVDE QALVQDEIEL
     VLQVNGKLRG ALKVPASADR AAIEAAALAS PELAKFAEGR TPKKVVVVPG RLVNVVV