ID   SYL_ACIBS               Reviewed;         874 AA.
AC   B0VKP9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=ABSDF2980;
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(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; CU468230; CAP02268.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VKP9; -.
DR   SMR; B0VKP9; -.
DR   EnsemblBacteria; CAP02268; CAP02268; ABSDF2980.
DR   KEGG; abm:ABSDF2980; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001741; 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..874
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091280"
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;  98024 MW;  6AEEF802D3C70895 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 IEECRIGSVA
     EADLATAEKK GMATGLFVKH PVTGEELPVW IANYVLMSYG SGAVMAVPAH DERDFEFANK
     FNLPIKQVID AKGADDADYS ATEWQEWYGS KEGKLVNSGE FDGLEFQAAF DAFLAKLEPQ
     GLANSKVQFR LRDWGVSRQR YWGCPIPMIN CDTCGQVTVP EDQLPVVLPT DVVPDGSGNP
     LNKMPEFYET KCPCCGGDAR RETDTLDTFV ESSWYYARYA SPDFTGGIVK PEAAKNWLPV
     NQYIGGVEHA ILHLLYARFF HKLMHDEGVV QGNEPFTNLL TQGMVLADTF YREAENGKKT
     WFNPANIELE 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