ID   SYL_RHIEC               Reviewed;         876 AA.
AC   Q2K2S7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=RHE_CH04116;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC92859.1; -; Genomic_DNA.
DR   RefSeq; WP_011427296.1; NC_007761.1.
DR   AlphaFoldDB; Q2K2S7; -.
DR   SMR; Q2K2S7; -.
DR   STRING; 347834.RHE_CH04116; -.
DR   PRIDE; Q2K2S7; -.
DR   EnsemblBacteria; ABC92859; ABC92859; RHE_CH04116.
DR   KEGG; ret:RHE_CH04116; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001936; 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; 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; Reference proteome.
FT   CHAIN           1..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009407"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   876 AA;  98000 MW;  79E5B43E3AEFEBD4 CRC64;
     MATERYNPRD AEPRWQQKWN EDKVFETDNS DPREKYYVLE MFPYPSGRIH MGHVRNYAMG
     DVVARYKRAR GYNVLHPMGW DAFGMPAENA AMERGVHPAS WTYQNIASMK AQLKAMGLSL
     DWSREFATCD VDYYQHQQHL FLDFLEKGLV YRKQSKVNWD PVDNTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKITDFS QELLDALDTL DQWPEKVRLM QKNWIGRSEG LTVRWEIVPE
     TAPAGETEIT VYTTRPDTLF GASFLAIAAD HPLAKDAAAK NVEIEAFCEE CRRAGTSLAA
     LETAEKKGLD TGIRVRHPLD PSWELPVYIA NFVLMDYGTG AIFGCPSGDQ RDLDFARKYG
     LPVVPVVMPT DGDAASFSVG DTAYDGEGVM INSRFLDGKT TEEAFNIVAD RLSAASLGNA
     PQGQRMINFR LRDWGISRQR YWGCPIPVIH CDACGVVPVP KKDLPVKLPE DVTFDQPGNP
     LDRHPTWRHV ACPNCGKDAR RETDTMDTFV DSSWYFTRFT APWEAKPTDP EAANRWLPVD
     QYIGGIEHAI LHLLYSRFFT RAMRETGHVA ATEPFKGLFT QGMVVHETYS RGAGASREWV
     APADIRIEEI DGKRRAFLLA SDEEVAIGSI EKMSKSKKNV VDPDDIIASY GADTARFFVL
     SDSPPERDVI WSEAGVEGAH RFTQRLWRLI SEAADCLSAV APAPASEGEA LTVSQAAHKT
     LKAVQNDYDK LWFNKAVARI YELVNALAAP LTRVAAGEGD IAYRAAVRDA AEILIQLVAP
     MTPHLAEECW AALGNAGLLA RTDWPRYDET LVMENDVVLP VQINGKKRAE LTISRDADQN
     AVTNAVLDLD AVKNALNGQA PKKIIVVPQR IVNIVV