ID   SYL_GEOSW               Reviewed;         805 AA.
AC   C5D6D7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=GWCH70_2764;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001638; ACS25453.1; -; Genomic_DNA.
DR   RefSeq; WP_015864859.1; NC_012793.1.
DR   AlphaFoldDB; C5D6D7; -.
DR   SMR; C5D6D7; -.
DR   STRING; 471223.GWCH70_2764; -.
DR   EnsemblBacteria; ACS25453; ACS25453; GWCH70_2764.
DR   KEGG; gwc:GWCH70_2764; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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   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; 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.
FT   CHAIN           1..805
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000202221"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   805 AA;  92561 MW;  EC08CF540D2FB8D9 CRC64;
     MSFNHREIEK KWQEYWEKNK TFKTVDDDDK PKFYVLDMFP YPSGAGLHVG HPEGYTATDI
     LARMKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNDPAEFT EKNINTFRRQ IKSLGFSYDW
     DREINTTDPN YYKWTQWIFL KLYEKGLAYM DEVPVNWCPA LGTVLANEEV IDGKSERGGH
     PVIRKPMKQW LLRITAYADR LLEDLEELDW PESVKEMQRN WIGRSEGAEI RFEVDGHDET
     FTVFTTRPDT LFGATYTVLA PEHPLVEKIT TPEQKAAVEA YLDAIKSKSD LERTDLAKEK
     TGVFTGAYAI HPVTGEKLPI WIADYVLMSY GTGAIMAVPA HDERDYEFAK KFNLPIKEVV
     AGGDIAKEAY TGDGEHINSD FLNGLNKEEA IKKMIEWLEA NGKGQKKVTY RLRDWLFSRQ
     RYWGEPIPII HWEDGTMTPV PEEELPLKLP KTDKIKPTGT GESPLANIEE WVNVVDPKTG
     KKGRRETNTM PQWAGSCWYY LRYIDPHNDK QLADPEKLKK WLPVDVYIGG AEHAVLHLLY
     ARFWHKFLYD IGVVPTKEPF QKLFNQGMIL GENNEKMSKS RGNVVNPDDI IESHGADTLR
     LYEMFMGPLE ASIAWSTKGL DGARRFLDRV WRLFVDENGN LNPKIVDNPE TDTLERVYHQ
     TVKKVTEDYE ALRFNTAISQ LMVFINEAYK APVLPKEYME GFVKLLSPVC PHIGEELWEK
     LGHNNTIAYE PWPTYDESKL VEEEVEIVVQ VNGKVRAKLR VPADISKEKL EQLAMEDEKI
     KEHIAGKTVR KVITVPGKLV NIVAN