SYL_LISMC
ID SYL_LISMC Reviewed; 803 AA.
AC C1KVV9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Lm4b_01673;
OS Listeria monocytogenes serotype 4b (strain CLIP80459).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=568819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP80459;
RX PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT "Comparative genomics and transcriptomics of lineages I, II, and III
RT strains of Listeria monocytogenes.";
RL BMC Genomics 13:144-144(2012).
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; FM242711; CAS05434.1; -; Genomic_DNA.
DR RefSeq; WP_003742319.1; NC_012488.1.
DR AlphaFoldDB; C1KVV9; -.
DR SMR; C1KVV9; -.
DR KEGG; lmc:Lm4b_01673; -.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR BioCyc; LMON568819:LM4B_RS08350-MON; -.
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..803
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000202223"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 575..579
FT /note="'KMSKS' region"
FT BINDING 578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 803 AA; 91939 MW; 0CBA3CA59982668F CRC64;
MTFNHKKMEP KWQQYWSEHN TFKTTEDKNK DNFYALDMFP YPSGAGLHVG HPEGYTATDI
LSRMKRMQGK NVLHPIGWDA FGLPAEQYAI DTGNDPEEFT ALNIANFTRQ IKSLGFSYDW
DREINTTDPE YYKWTQWIFE KLYEKGLAYE AEIAVNWCPA LGTVLANEEV IDGKSERGGF
PVFRKPMRQW MLKITAYADR LLDDLDLVDW PENIKDMQRN WIGRSEGAEV TFKIKDSDET
FNVFTTRPDT LFGATYTVFA PEHELIEKIT TPEQKEAVEA YKKQVELKSE LERTDLAKDK
TGVFTGAYAI NPINGEEVPI WIADYVLIQY GTGAIMAVPA HDERDFEFAQ QFGLNIRPVL
EGGDVTKEAF TGDGPHINSD FLNGLAKAEA ITAAIDWLEK EGIGSRKITY RLRDWLFSRQ
RYWGEPIPVI HWEDGETTLV PEDELPLLLP KATEIKPSGT GESPLANLHD WVNVTDKNGR
KGRRETNTMP QWAGSSWYFL RYIDPNNSEA IADKEKLAEW LPVDVYIGGA EHAVLHLLYA
RFWHKFLYDI GVVPTKEPFQ KLFNQGMILG ENNEKMSKSR GNVVNPDEVV EKYGADTLRL
YEMFMGPLEA SIAWNENGLE GARKFLDRIW RLLVTEEGTL AEKVTTDANA NLEKAYHHMV
KTVTNHYENL RFNTGISQLM IFINEAYKQD TIPKQYVEGF VQLLSPIAPH LAEELWEILG
HTETISYVAW PTYDETKLVE DEVEIVLQVN GKVKSKITVA KSLEKEELEK IAQEDNKMKE
NLEGKTIRKV IVVPGKLVNI VAN
