ID   SYL_RHILW               Reviewed;         876 AA.
AC   B5ZV40;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Rleg2_3924;
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304;
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(2010).
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; CP001191; ACI57186.1; -; Genomic_DNA.
DR   RefSeq; WP_012559382.1; NC_011369.1.
DR   AlphaFoldDB; B5ZV40; -.
DR   SMR; B5ZV40; -.
DR   STRING; 395492.Rleg2_3924; -.
DR   EnsemblBacteria; ACI57186; ACI57186; Rleg2_3924.
DR   KEGG; rlt:Rleg2_3924; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008330; 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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091351"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  97894 MW;  936E5BB1414FE104 CRC64;
     MATERYNPRD AEPRWQQKWN EDKVFETDNS DPREKYYVLE MFPYPSGRIH MGHVRNYAMG
     DVVARYKRAR GYNVLHPMGW DAFGMPAENA AMERGVHPAS WTYQNIGSMK AQLKAMGLSL
     DWSREFATCD VEYYQHQQHL FLDFLEKGLV YRKQSKVNWD PVDNTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKITDFS QDLLDALDTL DQWPEKVRLM QKNWIGRSEG LTIRWEIVAE
     TAPAGETEIT VYTTRPDTLF GASFLAIAAD HPLAKDAAAK NADIEAFCEE CRRAGTSLAA
     LETAEKKGMD TGIRVRHPLD PSWELPVYVA NFVLMDYGTG AIFGCPSGDQ RDLDFARKYG
     LPVVAVVMPQ DGDAASFSVG DTAYDGDGVM INSRFLDGKT TEEAFNIVAD RLSAASLGNT
     PQGERKVNFR LRDWGISRQR YWGCPIPVIH CDDCGVVPVP KKDLPVKLPD DVTFDQPGNP
     LDRHPTWRHV SCPTCGKDAR RETDTMDTFV DSSWYFTRFT APWEAKPTDP EAANRWLPVD
     QYIGGIEHAI LHLLYSRFFT RAMRETGHVA ATEPFKGLFT QGMVVHETYS RGAGGSREWV
     APADIRIEEI DGKRRALLLT TGEEIAIGSI EKMSKSKKNV VDPDDIIASY GADTARFFVL
     SDSPPERDVI WSEAGVEGAH RFTQRLWRLI SEAADALSAV APAPATEGEA LSISQAAHRT
     LKAVENDYDK LWFNKAVARI YELVNALAAP MTRVAAGEGD ATYRAAVRNA AEILIQLVAP
     MTPHLAEECW MALGNEGLLA RTGWPQYGET LVIENDVVLP VQINGKKRAE LTISRDADQN
     AVTNAVLDLD AVKNALNGQA PKKIIVVPQR IVNIVV