ID   SYL_ACIAD               Reviewed;         873 AA.
AC   Q6F817;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=ACIAD3106;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG69798.1; -; Genomic_DNA.
DR   RefSeq; WP_004924404.1; NC_005966.1.
DR   AlphaFoldDB; Q6F817; -.
DR   SMR; Q6F817; -.
DR   STRING; 62977.ACIAD3106; -.
DR   EnsemblBacteria; CAG69798; CAG69798; ACIAD3106.
DR   GeneID; 45235320; -.
DR   KEGG; aci:ACIAD3106; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; ASP62977:ACIAD_RS14025-MON; -.
DR   Proteomes; UP000000430; 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; Reference proteome.
FT   CHAIN           1..873
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151959"
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   873 AA;  97658 MW;  11032A965B307CED CRC64;
     MTTAHIDAEY QANAIESQIQ NDWENRKAFK VADTVEGKHR YILSMFPYPS GKLHMGHVRN
     YTIGDVISRF YRLKGETVLQ PMGWDAFGLP AENAAIAHQV APAKWTFENI AYMRDQLKKL
     GLSIDWDREF ATCTPEYYHW EQWLFVQLYK KGLIYRKLST VNWDPVDQTV LANEQVENGR
     GWRSGALVEK RDIPMYYFRI TDYAQELLDD LDTLKDGWPQ QVLTMQRNWI GRSTGMDITF
     PSANPEIYAD GLTVYTTRAD TLMGVTYVAV AAEHPMALKA AENNPELAAF IEECRMGSVA
     EADLATAEKK GMATGLFVKH PVTGEEVPVW IANYVLMSYG SGAVMAVPAH DERDFEFANK
     FNLPIKQVID AKAADDAEYS VTAWQEWYGS KEGTLVNSGE FDGLEFQAAF DAFLAKLEPQ
     GLANSKVQFR LRDWGVSRQR YWGCPIPMIN CDSCGQVPVP EEQLPVVLPT DVVPDGSGNP
     LNKMPEFYET TCPSCGGHAR RETDTLDTFV ESSWYYARYA SPDFTGGMVK PEAAQSWLPV
     NQYIGGVEHA ILHLLYARFF HKLMRDEGVV QGNEPFTNLL TQGMVLADTF YRESESGKKT
     WFNPADIILE RDEKGRIVSA KYSGDGQDVV IGGQEKMSKS KNNGIDPQAI IDQYGADTAR
     VFMMFAAPPD QSLEWSDAGV EGANRFLKRV WRLATGFLEK GYAQAPIAAE LSKDAQDLRR
     KTHETIQKVG DDIERRHAFN TAIAALMELL NATSKFEVQT ADDAAVAREA IETLLTLLAP
     FAPHLSQTLL AEFGIDLIAA QFPSVDESAL TRNTQTIVVQ VNGKLRGKLE VSVEISKDEL
     LAQAKALPEI QQFLTGPTKK EIVVPNKLVN LVV