ID   SYL_ACIC1               Reviewed;         832 AA.
AC   A0LSY4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Acel_0771;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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; CP000481; ABK52544.1; -; Genomic_DNA.
DR   RefSeq; WP_011719607.1; NC_008578.1.
DR   AlphaFoldDB; A0LSY4; -.
DR   SMR; A0LSY4; -.
DR   STRING; 351607.Acel_0771; -.
DR   EnsemblBacteria; ABK52544; ABK52544; Acel_0771.
DR   KEGG; ace:Acel_0771; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; DIDWADV; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008221; 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; 2.
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; 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..832
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334724"
FT   MOTIF           58..68
FT                   /note="'HIGH' region"
FT   MOTIF           598..602
FT                   /note="'KMSKS' region"
FT   BINDING         601
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   832 AA;  92222 MW;  68DA050860DB42E0 CRC64;
     MAGLGSPLGR LTAVTSEIYD FAAIQARWLP VWTELDPFRA SDDPSDPRER RYMLDMFPYP
     SGDLHMGHAE AFAIGDVVAR YWFQRGYNVL HPIGWDAFGL PAENAAIQRN LHPADWTYRN
     IETQAASFRN YAISFDWSRR LHTCDPEYYK WTQWLFLRLF ERGLAYRKAS PVNWCPNDQT
     VLANEQVVGG TCERCGAQVT KKTLTQWYFR ITEYAQRLLD DMALLEGRWP ERVLTMQRNW
     IGRSEGAYVD FTIEGRAEPV TVFTTRPDTL YGATFFVIAA DSPLAAEICA PEQRAAFEAY
     VDQVRRLSDI DRLSTERQKT GVFLGRYAVN PVNGERIPVW AADYVLADYG TGAIMAVPAH
     DQRDLDFALT YGLPVRVVVD TGEGDPAVTG VATEGDGVHI NSGLIDGTDK AEGIARITRY
     LEDIGKGRAG VTYRLRDWLV SRQRFWGAPI PIVHCPGCGE VAVPDQDLPV LLPDLRGADL
     APKGISPLAG AADWVQTTCP RCGGSAQRDT DTMDTFVDSS WYYLRYCSPH DPSQPFDVAK
     VRQWLPVHQY VGGVEHAILH LLYSRFITKV LHDMGLVDFV EPFSALLNQG QVINQGKAMS
     KSLGNGVDLG EQLATYGVDA VRLTMVFAGP PEEDIDWADM NPGALGKFLA RVWRIAGEVT
     SPVGAPPKDG DPALRRVTHR TIREVTELVE SFRFNVAVAR VMELANALRK AIDTGPGPAD
     PAVREGAEAL AVMLSLFAPY TAEECWARLG HQPTVAKAGW PTPDPELLAQ EEVTCVVQVN
     GKVRERLRVS PSISEEELRA AALAAPAVEK AIDGRPVQRI IVRAPKLVNV VV