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};
GN   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
//