ID   SYLB_AQUAE              Reviewed;         289 AA.
AC   O67646;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Leucine--tRNA ligase subunit beta;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase subunit beta;
DE            Short=LeuRS;
GN   Name=leuS'; OrderedLocusNames=aq_1770;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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   -!- SUBUNIT: Seems to consist of an alpha chain and a beta chain.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000657; AAC07608.1; -; Genomic_DNA.
DR   PIR; D70452; D70452.
DR   RefSeq; NP_214212.1; NC_000918.1.
DR   RefSeq; WP_010881149.1; NC_000918.1.
DR   AlphaFoldDB; O67646; -.
DR   SMR; O67646; -.
DR   STRING; 224324.aq_1770; -.
DR   EnsemblBacteria; AAC07608; AAC07608; aq_1770.
DR   KEGG; aae:aq_1770; -.
DR   PATRIC; fig|224324.8.peg.1366; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_1_1_0; -.
DR   InParanoid; O67646; -.
DR   OMA; SKHNTVD; -.
DR   OrthoDB; 1081178at2; -.
DR   BRENDA; 6.1.1.4; 396.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..289
FT                   /note="Leucine--tRNA ligase subunit beta"
FT                   /id="PRO_0000151963"
FT   MOTIF           45..49
FT                   /note="'KMSKS' region"
FT   BINDING         48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  33536 MW;  585B825AC6E3F606 CRC64;
     MKIKDFLQEN KISVGDNAIF LLEKLGIKDE NLIKFLEREI GESAKMSKSK ANVVDPEEAV
     EKYGADTVRL YILFAAPPEQ DFEWTDEGIQ GAYRFLQRYW NFVNKHLEKI KNLTYTVEEL
     RNVQGKAKEV RREIHQTIAD YRRDFEERYQ FNTAIAKIMK LLNTLQDFSP QTEQDYKVLR
     EGIETITLLL SPITPHIAEE VWEMLGNEGF IINQPIPEPD PEALKVEEIE IPVQVNGKLR
     ARVKVPADAD EETVKNIVLS DERVQKWVQG KEVKKFIYVK GKLVNVVVK