SYL_CLOBH
ID SYL_CLOBH Reviewed; 813 AA.
AC A5HY79; A7G094;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=CBO0186, CLC_0240;
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(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; CP000727; ABS36860.1; -; Genomic_DNA.
DR EMBL; AM412317; CAL81738.1; -; Genomic_DNA.
DR RefSeq; WP_011948005.1; NC_009698.1.
DR RefSeq; YP_001252730.1; NC_009495.1.
DR RefSeq; YP_001386143.1; NC_009698.1.
DR AlphaFoldDB; A5HY79; -.
DR SMR; A5HY79; -.
DR GeneID; 5187707; -.
DR KEGG; cbh:CLC_0240; -.
DR KEGG; cbo:CBO0186; -.
DR PATRIC; fig|413999.7.peg.184; -.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR PRO; PR:A5HY79; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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; 2.
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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..813
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009326"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 572..576
FT /note="'KMSKS' region"
FT BINDING 575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 813 AA; 92912 MW; F4DECBDF3244DC0D CRC64;
MGNYSTKIDE KWQKKWEENS LYKFNNKNLD KKLYVLEMFS YPSGSKLHAG HWFNYGPVDS
WARFKRMQGY NVFQPMGFDA FGLPAENYAI KTGIHPKDST FKNIETMETQ LKAMGAMFNW
ENEVITCSPD YYKWTQWLFL KLYEKGLAYK KKAPVNWCPS CNTVLANEQV LDGKCERCDS
NVDKKNLEQW FLKITDYADE LLEKLDELDW PEKTKAMQKH WIGKSVGAEV TFNVADSDLS
FNVFTTRVDT LFGVTYVVLA PENDLVDKLT TPENKAEVES YKTQAKNQSD IERQSITREK
TGVFSGSYAI NPINGKKVPI WIGDYVLNTY GTGCVMAVPA HDERDFAFAT KYNLPIERVI
EGGDSLPYTE YGGMVNSGEF DGLLGNEAKE AVISKLESMN LGRKKINYRL RDWLVSRQRY
WGAPIPIIYC EKCGTVEVPI EQLPVELPYN VEFSPDGKSP LGKCDDFINT TCPKCGGPAK
READTLDTFV CSSWYYLRYP DNNNEKDAFN PELINKMLPV DKYVGGPEHA CMHLLYARFI
TKALRDMGYL NFDEPFLSLT HQGLILGPDG LKMSKSKGNT ISPDDYIKEF GADVFRMYLM
FGFDYTEGGA WSDDAIKSIG KFVDRVERIL ENAREEIKNS KDNKSTMDKD EKELNYVRHH
SIKSITEDID KMQFNTSIAR LMEFTNALSK YLGIDAIKNA LFLRESIIDF ITLLAPFAPH
FAEEQWKLIG INSSIFNEKW PEFDPKALIK DEVEIAVQVN GKIRAKINIS TSSSEDEIKE
SALNNEDIKN SIGDKEIKKV IVIKNRLVNI VAK
