SYL_BACCQ
ID SYL_BACCQ Reviewed; 802 AA.
AC B9J1E1;
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=BCQ_4553;
OS Bacillus cereus (strain Q1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1;
RX PubMed=19060151; DOI=10.1128/jb.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(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; CP000227; ACM14979.1; -; Genomic_DNA.
DR RefSeq; WP_000009457.1; NC_011969.1.
DR AlphaFoldDB; B9J1E1; -.
DR SMR; B9J1E1; -.
DR EnsemblBacteria; ACM14979; ACM14979; BCQ_4553.
DR GeneID; 59158966; -.
DR GeneID; 64203344; -.
DR KEGG; bcq:BCQ_4553; -.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000441; 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 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; 1.
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.
FT CHAIN 1..802
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199180"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 576..580
FT /note="'KMSKS' region"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 802 AA; 91359 MW; 7A1DB4F78DD133B8 CRC64;
MSFNHQEIEK KWQGYWEENK TFRTPDETEK PKFYALDMFP YPSGAGLHVG HPEGYTATDI
LSRMKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNSPAEFT EHNINTFRNQ IKSLGFSYDW
DREVNTTDPN YYKWTQWIFL KLFEKGLAYV DEVPVNWCPA LGTVLANEEI IDGKSERGGH
PVERRPMRQW MLKITAYGDR LLEDLDELDW PESLKDMQRN WIGRSEGAEV HFNIDGTDEK
FTVFTTRPDT LFGASYCVLA PEHALVADIT TAEQKEAVEA YINSVKMKSD LERTELAKEK
TGVFTGAYAV NPVNGEKLPI WIADYVLATY GTGAVMAVPA HDERDYEFAS TFNLPMKEVV
KGGDITKEAY TGDGEHVNSA FLDGLNKEEA IAKMIEWLEV TSAGNQKVTY RLRDWLFSRQ
RYWGEPIPVI HWEDGTMTAV KEEELPLVLP KTDNIRPSGT GESPLANIDE WVNVVDPETG
KKGRRETNTM PQWAGSCWYY LRYIDPNNSE ALVDPEKVKQ WLPVDIYIGG AEHAVLHLLY
ARFWHKVLYD IGVVPTKEPF QQLFNQGMIL GENNEKMSKS KGNVVNPDDI VASHGADTLR
LYEMFMGPLD ASIAWSENGL DGARRFLDRV WRLFVQDNGE LSEKITDAPN KELEKAYHQT
VKKVTEDYAE LRFNTAISQM MVFINDAYKA ETLPKEYVEG FVKMIAPVAP HIGEELWSKL
GYNETITYAS WPTFDESKLV EDEVEIVVQV MGKVRAKLTM SKDASKEEME QLALEAIKDQ
IEGKTVRKVI VVPGKLVNVV AN
