SYL_BACC2
ID SYL_BACC2 Reviewed; 802 AA.
AC B7IL05;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=BCG9842_B0386;
OS Bacillus cereus (strain G9842).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405531;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9842;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus G9842.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001186; ACK97313.1; -; Genomic_DNA.
DR RefSeq; WP_000009438.1; NC_011772.1.
DR AlphaFoldDB; B7IL05; -.
DR SMR; B7IL05; -.
DR EnsemblBacteria; ACK97313; ACK97313; BCG9842_B0386.
DR KEGG; bcg:BCG9842_B0386; -.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000006744; 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_1000199179"
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; 91365 MW; 1CAAD585E9C6031B CRC64;
MSFNHQDIEK KWQGYWEENK TFRTPDETEK PKFYALDMFP YPSGAGLHVG HPEGYTATDI
LSRMKRMQGY KVLHPMGWDA FGLPAEQYAL DTGNSPAEFT EHNINTFRNQ IKSLGFSYDW
DREVNTTDPN YYKWTQWIFL KLFEKGLAYV DEVPVNWCPA LGTVLANEEI IDGKSERGGH
PVERRPMRQW MLKITAYGDR LLEDLDELDW PESLKDMQRN WIGRSEGAEV HFNIDGTDEK
FTVFTTRPDT LFGATYCVLA PEHALVAEIT TAEQKEAVEA YINAVKMKSD LERTELAKEK
TGVFTGAYAV NPVNGEKLPI WIADYVLATY GTGAVMAVPA HDERDYEFAS VFNLPMKEVV
KGGDITKEVY TGDGAHVNSA FLDGLNKEEA IAKMIEWLEV TSAGNQKVTY RLRDWLFSRQ
RYWGEPIPVI HWEDGTMTAV KEEELPLVLP KTENIRPSGT 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 WPIFDESKLV EDEVEIVVQV MGKVRAKLTM SKDASKEEME QLALEAIQDQ
IEGKTVRKVI VVPGKLVNVV AN