ID   SYL_GRABC               Reviewed;         875 AA.
AC   Q0BW99;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 112.
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=GbCGDNIH1_0005;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI60903.1; -; Genomic_DNA.
DR   RefSeq; WP_011630713.1; NC_008343.2.
DR   AlphaFoldDB; Q0BW99; -.
DR   SMR; Q0BW99; -.
DR   STRING; 391165.GbCGDNIH1_0005; -.
DR   KEGG; gbe:GbCGDNIH1_0005; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001963; 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..875
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334761"
FT   MOTIF           57..67
FT                   /note="'HIGH' region"
FT   MOTIF           631..635
FT                   /note="'KMSKS' region"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   875 AA;  97795 MW;  91357A96A7461C7D CRC64;
     MTDSITDLQS DQRPDRSYDF ASAERRWQLA WTERACFTVP DVPDPGARTY YVLEMFPYPS
     GQIHMGHVRN YTLGDVVARY KRAQGYQVLH PMGWDAFGLP AENAARERGV HPGQWTWNNI
     AAMRGELQRM GLSITWEREF ATCDPSYYGH QQALFLDFLK KNLVERRESW VNWDPVDETV
     LANEQVIDGK GWRSGAPVER KKLSQWFLRI TDYAEELLAG LDQLDRWPER VRVMQSRWIG
     RSEGARLRFP LVEPLGDQRE IEVYTTRPDT LYGMSFVAIA ADHPVAAALA AHHPALAAFV
     AECRSLGTSE AAIEAAEKRG FDTGLRVKHP FCDETFPVWI ANFVLMDYGT GAVFGCPAHD
     QRDLDFARKY DLSVTPVVLP SDQDAASFTI GRKAYDGDGI LFNSGPFDGL TPDAARREAI
     TRLEAMGWGQ GVTNWRLRDW GVSRQRYWGC PIPIIHCDQC GPVPVPADQL PVTLPEDVTF
     DRPGNPLDHH PSWKHVTCPS CGAAAVRETD TFDTFVDSSW YFARFASPHA HVPVLKEAAQ
     NWLPVDQYIG GIEHAILHLL YARFFTRAMA DTGHVPVREP FAGLFTQGMV THESYRAADG
     RWLSPVEVTR HGETVVETAT GEPVQVGRGE KMSKSKRNTV APGEIFNRYG ADAARWFILS
     DNPPERDMEW TDAGAVGAYR FVQRLYRLAE AVARIAKEET NRDDASSDAA MTLRRMTHRT
     VAAVTEALEG FNFNVAVARV YEFANALTEA EKKAAEPGMT AARVEAITLL SRIIAPMMPH
     LAEEMATLIE QGPKLVAEQV WPSADPALLV VQSVTIAIQV MGKLRATLDI SPDADQDSVI
     AQAEADPNVV RALEGKRVVK RIYVPNRIVN FVIAG
//