SYL_PSEAB
ID SYL_PSEAB Reviewed; 873 AA.
AC Q02SF5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, 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}; OrderedLocusNames=PA14_12230;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ13262.1; -; Genomic_DNA.
DR RefSeq; WP_003137700.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02SF5; -.
DR SMR; Q02SF5; -.
DR PRIDE; Q02SF5; -.
DR EnsemblBacteria; ABJ13262; ABJ13262; PA14_12230.
DR KEGG; pau:PA14_12230; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR BioCyc; PAER208963:G1G74-1017-MON; -.
DR Proteomes; UP000000653; 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 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_1000009398"
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; 97650 MW; C3CCEB1C5DD016F2 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 DDFESSVWKE WYGAKDESVL TVNSGKYDNL GYQAAFDAIG ADLEAKGLGQ
ARTQFRLRDW GISRQRYWGC PIPIIHCEAC GDVPVPADQL PVVLPEDVVP DGSGSPLAKM
PEFYECSCPK CGQPAKRETD TMDTFVESSW YFARYACPQF EGGMLDRKAA DYWLPVDQYI
GGIEHAILHL LYARFFHKLM RDEGLVGSDE PFKNLLTQGM VVADTYYRTT ANGGKDWFNP
ADVEVERDAK AKVVGARLKS DGQPVEIGGT EKMSKSKNNG VDPQSMIDQY GADTCRLFMM
FASPPDMSLE WSDAGVEGAN RFLRRVWRLA HAHVSAGLPG ALDVAALDDA QKQVRRAIHL
AIRQASQDVG QHHKFNTAIA AVMTLMNVLE KAPNQDAQDR ALIQEGLETV VLLLAPITPH
ICHVLWGQLG HAEAVIDARW PSVDESALVQ DTLQLVVQVN GKLRGHIDVA ASASREDVEA
AARANENVLR FTEGLSIRKV IVVPGKLVNI VAN
