ID   SYL_STUS1               Reviewed;         868 AA.
AC   A4VQZ0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   27-MAR-2024, entry version 100.
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};
GN   OrderedLocusNames=PST_3768;
OS   Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Stutzerimonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP81391.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000304; ABP81391.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_013984164.1; NC_009434.1.
DR   AlphaFoldDB; A4VQZ0; -.
DR   SMR; A4VQZ0; -.
DR   GeneID; 66823030; -.
DR   KEGG; psa:PST_3768; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   Proteomes; UP000000233; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..868
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334796"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           627..631
FT                   /note="'KMSKS' region"
FT   BINDING         630
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   868 AA;  96723 MW;  536449476BCBD0FE CRC64;
     MHEQYQPREI EAAAQSHWDS QKSFEVSEQP GKDTFYCLSM FPYPSGKLHM GHVRNYTIGD
     VIARYQRMQG KNVLQPMGWD AFGMPAENAA MKNQVAPAKW TYENIAYMKA QLKSLGLAID
     WSREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG
     ALIEKREIPM YYFKITAYAD ELLESLDELD GWPEQVKTMQ RNWIGKSRGM EISFPYDVAS
     IGNEGVMKVF TTRPDTLMGA TYVAVAAEHP LATLAAQHNP ELQAFIDECK RGGVAEADIA
     TQEKKGLATS LRVQHPLTGE LLPVWVANYV LMNYGEGAVM AVPAHDERDF EFASKYGLPI
     KPVVRTSAGD ETPAPWQDAY GEHGQLINSG IYDGLDFEGA FDAIEVALQK KGLGQARTQF
     RLRDWGISRQ RYWGCPIPII HCDSCGDVPV PEDQLPVVLP EDVVPDGAGS PLARMPEFYE
     CTCPKCGAPA KRETDTMDTF VESSWYFARY ASPNYDKGMV DPQAANHWLP VDQYIGGIEH
     AILHLLYARF FHKLMRDEGL VSSNEPFKNL LTQGMVVAET YYRTLENGGK DWFNPADVEV
     ERDAKAKVIG ARLKTDGLPV EIGGTEKMSK SKNNGVDPQA MIDAYGADTC RLFMMFASPP
     DMSLEWSDSG VEGASRFLRR VWRLAHAHVS AGLPGALDVA ALNDEQKAVR RAIHLAIKQA
     STDVGQHHKF NTAIAQVMTL MNVLEKAPTA GEQDRALLQE GLETVALLLA PITPHICHEL
     WQQLGKPGAI IDAQWPKVDE AALVQDSLTL VVQVNGKLRG QIEVPASASR EEVETAARGN
     ENVLRFTEGL TIRKVIVVPG KLVNIVAN
//