ID   SYL_AGRVS               Reviewed;         876 AA.
AC   B9JV46;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Avi_4381;
OS   Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain
OS   S4)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=311402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 / ATCC BAA-846;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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; CP000633; ACM38184.1; -; Genomic_DNA.
DR   RefSeq; WP_015917594.1; NC_011989.1.
DR   AlphaFoldDB; B9JV46; -.
DR   SMR; B9JV46; -.
DR   STRING; 311402.Avi_4381; -.
DR   EnsemblBacteria; ACM38184; ACM38184; Avi_4381.
DR   KEGG; avi:Avi_4381; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001596; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199171"
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;  97494 MW;  C5CD367D9EC31F3A CRC64;
     MSTERYNPRD AEPRWQEKWS EAKIFETDNN DPREKYYVLE MFPYPSGRIH IGHVRNYAMG
     DVVARYKRAR GYNVLHPMGW DAFGMPAENA AMQNKVHPKD WTYQNIASMR AQLKSMGLSL
     DWSREFATCD VEYYQRQQYL FLDMMEKGLV YRKQSKVNWD PVDQTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKITDFA QDLLDALDTL DHWPEKVRLM QKNWIGRSEG LAIRWEIAAG
     TGPQGFTDVQ VYTTRPDTLF GASFLAIAAD HPLAKALSET SSDIAAFCDE CRRAGTSLAA
     LETAEKKGLD TGIKVKHPLD PAWELPVYIA NFVLMDYGTG AIFACPSGDQ RDLDFARKYG
     LPVVPVVMPR DGDAASFTVG DTAYDGDGVM INSRFLDGLT TQEAFDVVAG KLTAAQLGNE
     PVAERRVNFR LRDWGVSRQR YWGCPIPVIH CDDCGVVPVP KQDLPVKLPD DVTFDVPGNP
     LDRHPTWRNV SCPCCGKAAR RETDTMDTFV DSSWYYTRFT APWEDKPTDP AVANHWLPVD
     QYIGGIEHAI LHLLYSRFFT RAMRETGHVA VSEPFKGLFT QGMVVHETYR LGSGANGQWV
     APADIRVEDV DGARRAFLLS SGEEVTIGSV EKMSKSKKNV IDPDDILGSY GADTARFFVL
     SDSPPDRDVI WSEAGIEGSH RFVQRLWRLV SEAADVLRTS ASTPAKDGAG RAVSQAAHKT
     LQAVGADLDK LAFNKAVARI YELLNTLAAP LTQVASGNAD TSFVAAVRNA TEILIQIIAP
     MMPHLAEECW AVLGHSGMVS QADWPVFHAE LVAENEVVMP VQINGKKKAE LTIGRDADQN
     AVSQAVLDLD AVKAALQGQT PKKIIVVPQR IVNIVV