SYL_PSEA8
ID SYL_PSEA8 Reviewed; 873 AA.
AC B7V9C9;
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}; OrderedLocusNames=PLES_09881;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(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; FM209186; CAW25715.1; -; Genomic_DNA.
DR RefSeq; WP_012613615.1; NC_011770.1.
DR AlphaFoldDB; B7V9C9; -.
DR SMR; B7V9C9; -.
DR PRIDE; B7V9C9; -.
DR KEGG; pag:PLES_09881; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
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 Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR43740; PTHR43740; 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; 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..873
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199219"
FT REGION 624..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 632..636
FT /note="'KMSKS' region"
FT BINDING 635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 873 AA; 97678 MW; 4CBC246D189F69D7 CRC64;
MHEQYQPLEI ETQAQNYWKE HQSFLVRELP DKEKFYCLSM FPYPSGKLHM GHVRNYTIGD
VISRYHRMQG RNVLQPMGWD AFGMPAENAA MKNNVAPAAW TYDNIAYMKS QLDSLGLAID
WSREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG
ALIEKREIPM YYFKITAYAE ELLESLDNLP GWPEQVKTMQ RNWIGKSRGM EIGFPYDQAS
IGHAGQLKVF TTRPDTLMGA TYVAVAAEHP LATQAAQNDP QLQAFIDECK RGGVAEADIA
TQEKKGMATS LFVEHPLTGD KLPVWVANYV LMNYGEGAVM AVPGHDERDF EFANKYGLPI
RQVIAKVEGD NDFESSVWKE WYGAKDESVL TVNSGKYDNL GYQAAFDAIG ADLEAKGLGQ
ARTQFRLRDW GISRQRYWGC PIPIIHCEAC GDVPVPADQL PVVLPEDVVP DGSGSPLAKM
PEFYECNCPK CGQPAKRETD TMDTFVESSW YFARYACPQF EGGMLDRKAA DYWLPVDQYI
GGIEHAILHL LYARFFHKLM RDEGLVGSDE PFKNLLTQGM VVADTYYRTT ANGGKDWFNP
ADVEVERDAK AKVVGARLKS DGQPVEIGGT EKMSKSKNNG VDPQSMIDQY GADTCRLFMM
FASPPDMSLE WSDAGVEGAN RFLRRVWRLA HAHVSAGLPG ALDVATLSDA QKQVRRAIHL
AIRQASQDVG QHHKFNTAIA AVMTLMNVLE KAPNQDAQDR ALIQEGLETV VLLLAPITPH
ICHVLWGQLG HAEAVIDARW PSVDESALVQ DTLQLVVQVN GKLRGHIDVA ASASREDVEA
AARANENVLR FTEGLSIRKV IVVPGKLVNI VAN
