ID   SYL_RHOP2               Reviewed;         874 AA.
AC   Q2J364;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=RPB_0385;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-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; CP000250; ABD05096.1; -; Genomic_DNA.
DR   RefSeq; WP_011439286.1; NC_007778.1.
DR   AlphaFoldDB; Q2J364; -.
DR   SMR; Q2J364; -.
DR   STRING; 316058.RPB_0385; -.
DR   EnsemblBacteria; ABD05096; ABD05096; RPB_0385.
DR   KEGG; rpb:RPB_0385; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008809; 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; 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..874
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009409"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           630..634
FT                   /note="'KMSKS' region"
FT   BINDING         633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   874 AA;  97628 MW;  C5CB05782C840BC2 CRC64;
     MSNERYNARE SEPKWQAKWD EAKIFATRND DPRPKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVVARTMRAR GHNVLHPMGW DAFGLPAENA AIERKVAPKA WTYDNIASMK KQLQTMGLSL
     DWAREFATCD PTYYKHQQKM FLDFLKVGLA ERETRKLNWD PVDMTVLANE QVIDGRGWRS
     GAVVEQREMN QWVFKITRYA QDLLDALETL DRWPDKVRLM QRNWIGRSEG LLVRFALDAA
     TTPAGETELK IFTTRPDTLF GAKFMAIAPD HPLAQAAAAK NEKIAAFVEE CKKRGTAQAE
     IDTAEKQGID TGIRALHPFD PTWQIPVYVA NFVLMEYGTG AIFGCPAHDQ RDLDFVNKYQ
     LGNTPVVCPE GQDPLSFVIT DEAYDGDGRL INSRFLDGMS IADAKEEVAK RLETATLGNA
     PVGERKVNFR LRDWGISRQR YWGCPIPVIH CEVCGVVPVP DKDLPVVLPE DVSFDKPGNA
     LDHHPTWKHV PCPQCGGKAQ RETDTMDTFV DSSWYFARFT DPWNETAPTT PDVVNRMLPV
     DQYIGGVEHA ILHLLYSRFF TRAMKATGHL GLDEPFRGMF TQGMVVHETY RTADGHFASP
     AEVAIVAEGD GRRATLLDGG TPVEIGPIEK MSKSKRNTVD PDDIIGSYGA DTARWFMLSD
     SPPDRDVIWS EEGVKGASRF VQRLWRMVND AAAIARSAPA ERPATFGPEA LAVRKAAHGA
     LDKVLSGIER LAFNVSLAHI REFANSFGEA LAKPGQPSPD LAWAIREAAV ILVQLFHPMM
     PHLAEECWAA LGRPGLVSEA LWPQIERDLL VEDSITLPVQ VNGKKRGDIT VARDANTQEI
     EAAVLALDAV RQALDGKPVR KVIVVPQRIV NVVG