ID   SYL_RHOPB               Reviewed;         882 AA.
AC   Q21CM7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=RPC_0284;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) 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; CP000301; ABD85859.1; -; Genomic_DNA.
DR   RefSeq; WP_011470767.1; NC_007925.1.
DR   AlphaFoldDB; Q21CM7; -.
DR   SMR; Q21CM7; -.
DR   STRING; 316056.RPC_0284; -.
DR   EnsemblBacteria; ABD85859; ABD85859; RPC_0284.
DR   KEGG; rpc:RPC_0284; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
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   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..882
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009411"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           634..638
FT                   /note="'KMSKS' region"
FT   BINDING         637
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   882 AA;  98244 MW;  07E5065633EE7FAB CRC64;
     MTNERYNARE SEPRWQRQWD DNAIFATQND DPRPKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVVARTMRAR GYNVLHPMGW DAFGMPAENA AMANKVHPKS WTYANIATMK AQLKSMGLSL
     DWSREFATCD PSYYKHQQRM FIDFLAAGLV ERKQSKVNWD PVDNTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKISKYS EDLLTALDRL DRWPDKVRIM QRNWIGRSEG LLLRFALDTS
     TTPNHETEVE VFTTRPDTLF GAKFVALSPD HPLAAEAAKS NPALAAFIEE CRKTGTAQAE
     IDTAEKQGFD TGIRAVHPFD PSWQLPVYVA NFVLMDYGTG AIFGCPAHDQ RDLDFVNKYG
     LGNLPVVCPE GQDPATFVVT DIAYDGDGRL INSNNGFIAL DGMSIADAKE AVAKRLEAIA
     LGNRPVAQRQ VNFRLRDWGI SRQRYWGCPI PIIHCEVCGV VPVPIKDLPV KLPDDIEFDR
     PGNPLDRHPT WKHVACPQCG GKARRETDTM DTFVDSSWYF SRFTDPWNED APTTRAVVDR
     MMPVDQYIGG VEHAILHLLY SRFFTRAMQA TGHVGFDEPF RGMFTQGMVV HETYRKLDGT
     FASPAEIRIV ADGDNRLASL LDSGQPVEIG PIEKMSKSKR NTVDPDDIIG SYGADTARWF
     MLSDSPPDRD VIWSEDGVKG ASRFVQRVWR LVSAMAPQLP APGTRLDAAN HPAAQALRVA
     AHRTLSEILA GIDRLRFNTA VAKLYVYVGE LEAVLANAPQ GGLGGDPVLA AAAREAIDIL
     VLLIAPMMPH LAEECWAAIG HSGLVSEARW PEIETALLVS DSITLPVQVN GKKRGEVTVA
     RDAQNPQIEA AVLALDAVKQ ALDGKPVRKI IIVPQRIVNV VG