ID SYL_ACIB5 Reviewed; 874 AA.
AC B7I5I5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=AB57_0622;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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; CP001182; ACJ40043.1; -; Genomic_DNA.
DR RefSeq; WP_000155773.1; NC_011586.2.
DR AlphaFoldDB; B7I5I5; -.
DR SMR; B7I5I5; -.
DR GeneID; 66398499; -.
DR KEGG; abn:AB57_0622; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR Proteomes; UP000007094; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..874
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199169"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 636..640
FT /note="'KMSKS' region"
FT BINDING 639
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 874 AA; 98080 MW; 001491487750CA03 CRC64;
MTISHIDPEY QANTIEPSVQ QDWENRKVFK VADTVEGKHR YILSMFPYPS GKLHMGHVRN
YTIGDVISRF YRLKGETVLQ PMGWDAFGLP AENAAIAHKV APAKWTFENI AYMRDQLKKL
GLSVDWDREF ATCTPEYYHW EQWLFVQLYK KGLIYRKLST VNWDPVDQTV LANEQVENGR
GWRSGALVEK RDIPMYYFRI TDYAQELLDD LDTLQDGWPQ QVLTMQRNWI GRSTGMEITF
PSANTEIYAD GLTVYTTRAD TLMGVTYVAV AAEHPLALKA AENNPELAAF IEECRMGSVA
EADLATAEKK GMATGLFVKH PVTGEELPVW IANYVLMSYG SGAVMAVPAH DERDFEFANK
FNLPIKQVID AKGADDADYS ATEWQEWYGS KEGKLVNSGE FDGLEFQAAF DAFLAKLEPQ
GLANSKVQFR LRDWGVSRQR YWGCPIPMIN CDTCGQVTVP EDQLPVVLPT DVVPDGSGNP
LNKMPEFYET KCPCCGGDAR RETDTLDTFV ESSWYYARYA SPDFTGGMVK PEAAKNWLPV
NQYIGGVEHA ILHLLYARFF HKLMRDEGVV QGNEPFTNLL TQGMVLADTF YREAENGKKT
WFNPADIELE RDEKGRIISA KYSGDGQEVI IGGQEKMSKS KNNGIDPQAI IDQYGADTAR
VFMMFAAPPD QSLEWSDAGV EGANRFLKRV WRLVASFLEK GNSATAIDKA NLSKDAQDLR
RKTHETIQKV SDDIERRHAF NTAIAALMEL LNASNKFEAK DDNDVAVERE AITTLLTLLA
PFAPHLSQTL LAQFGTDLTE ATFPEVDASA LTRNTQTIVV QVNGKLRGKL EVSVDISKDE
LLAQAKALPE VQQFLTGPTK KEIVVPNKLV NLVV
//
