ID   SYL_POLNS               Reviewed;         890 AA.
AC   B1XT72;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-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=Pnec_0254;
OS   Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=452638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STIR1;
RX   PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA   Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA   Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT   "Polynucleobacter necessarius, a model for genome reduction in both free-
RT   living and symbiotic bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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; CP001010; ACB43549.1; -; Genomic_DNA.
DR   RefSeq; WP_012357316.1; NC_010531.1.
DR   AlphaFoldDB; B1XT72; -.
DR   SMR; B1XT72; -.
DR   STRING; 452638.Pnec_0254; -.
DR   EnsemblBacteria; ACB43549; ACB43549; Pnec_0254.
DR   KEGG; pne:Pnec_0254; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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; 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; PF00133; tRNA-synt_1; 2.
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.
FT   CHAIN           1..890
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091342"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           645..649
FT                   /note="'KMSKS' region"
FT   BINDING         648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   890 AA;  99540 MW;  2CCD3CC373DE5E60 CRC64;
     MSKDYDYRSI EAAAQADWEG AQVYQVAENA VDAQGKKKSK YYACSMLPYP SGKLHMGHVR
     NYTINDVMAR QLRMQGYNVL MPMGWDAFGM PAENAAIQNK VPPAKWTYDN IAYMKKQMAA
     MGLAIDWSRE VATCNPDYYR WNQWLFLKML EKGIAYRKTQ VVNWDPIDQT VLANEQVIDG
     RGWRSGALVE KREIPGYYFN ITAYAEPLLS GLDGLGWPER VKTMQQNWIG KSRGVRFAFK
     HEIADDYGNF IQDGLLYVFT TRADTIMGVT FCAVAAEHPL ATKAAANNSA LAAFIEKCKT
     GSVIEADLAT QEKEGMFTGL YVTHPLTYEP VPVWVGNYVL MSYGDGAVMG VPAHDERDFA
     FALKYELPIK QVIALKDESP MFNATCWEDW YAQKDGVVCF NSAQFDGLSH EEAVSAVAKA
     LEKLGIGDIK TSFRLRDWGI SRQRYWGTPI PIIHCGDESN PGCGAVPVPE ADLPVVLPED
     CVPDGSGNPL NKRADFLSVK CPKCGKPARR ETDTMDTFVD SSWYFMRYTG PNAKTMVDER
     NEYWMPMDQY IGGIEHAILH LLYARFWTKI MRDLNLITFD EPFQNLLTQG MVLNETYYSE
     DASGKKTWLN PLDVELDLDE KGRPKGAKLI GDTLNTPVVV GGVEKMSKSK NNGVDPQALI
     DEYGADTARL FVMFAAPPEQ QLEWSGAGVD GASRFLRRVW MYFSGQASAL RDASDSLPSN
     LNDAEKELRR EVHTILKQAN FDYQRRQYNT VVSAAMKMLN ILEPIKLDQN AAISAPVLRE
     CLSILLRVLY PVVPHLTHVL WKEVGYAKTM GPLLDAPWPT VDEATLVQTE ITLMLQINGK
     LRGDIKVPAD ANKEQVEALA LQSEPAQKAL NGGAPKKVIV VPGRLVNIVA