ID   SYL_UREU1               Reviewed;         806 AA.
AC   B5ZBI3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=UUR10_0380;
OS   Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=565575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33699 / Western;
RA   Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT   "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL   Submitted (OCT-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; CP001184; ACI60167.1; -; Genomic_DNA.
DR   RefSeq; WP_012560305.1; NC_011374.1.
DR   AlphaFoldDB; B5ZBI3; -.
DR   SMR; B5ZBI3; -.
DR   STRING; 565575.UUR10_0380; -.
DR   EnsemblBacteria; ACI60167; ACI60167; UUR10_0380.
DR   GeneID; 45015927; -.
DR   KEGG; uue:UUR10_0380; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_14; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002018; 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; 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; 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.
FT   CHAIN           1..806
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091376"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           580..584
FT                   /note="'KMSKS' region"
FT   BINDING         583
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   806 AA;  93235 MW;  F067C46230A60CBB CRC64;
     MYNHNKIEKK WQKYWLDNKT FKFVDNPNNP KKFYVLDMFP YPSGKGLHVG HPKGYTATDV
     ISRFKRLNGY DVLHPIGWDA FGLPAEQYAL ETNNHPHTFT QQNIKIFRKQ LQMIGFDFDY
     DKEVDTTDPQ FYQWTQWIFV QLYKHNLAEI QDIDVNWCEN LGTVLSNEEV VLNDKNERVS
     ERGGHPVVRK PMKQWVLKIV DYADKLLDGL NEVEFSESLK SLQRNWIGKS IGTNVQFKIK
     DSHLALDVFT TRIDTIYGAQ YLVVAPEHPI LKSIVSEQQA SVVQAYVDQT KKISDLDRIA
     DTNKTGVFSG TYAINPINQE IIPIWVSDYV LMNFATGAVM GVPAHDERDY AFAKKYDLPI
     KSVIDTKQSL PYTGDGLHIN SPMINGLNIE QSQNILNDYL VKNHLAKRVV NYKLRNWIFS
     RQRYWGEPFP VLFDENNQIK IIEDLPVLLP NLDEFKPSKT GESPLANAQE WLYVEIDGKK
     YRRETNTMPQ WAGSSWYFLA YILKNEDGSY TPLNSEEAKK RFAKWLPVDV YIGGQEHAVL
     HLLYARFWHR FLYDIGVVPT KEPFYKVINQ GMILGENNEK MSKSKGNVIN PDDIIASHGA
     DTLRIYEMFM GPLTASLPWS PDGLDAMRKW LDRVYRLYHN LSELEVVEDV NKLNEEIIIT
     YHTLIKNYTK AINEQAFNIA ISEMMVFVNV LYKNKVINYK LLDNFLILLS CFAPHLAEEL
     YSLNHSESVC LQKMPIYDEQ KIIAQNVTIP IQINGKLKHT INVLRDTNAE QLINLALACE
     QVKQAIGDQP IKKQIVVVNK IINFVI