ID   SYK_BORBU               Reviewed;         521 AA.
AC   O51603;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Lysine--tRNA ligase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysyl-tRNA synthetase;
DE            Short=LysRS;
GN   Name=lysS; OrderedLocusNames=BB_0659;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=9405621; DOI=10.1073/pnas.94.26.14383;
RA   Ibba M., Bono J.L., Rosa P.A., Soell D.;
RT   "Archaeal-type lysyl-tRNA synthetase in the Lyme disease spirochete
RT   Borrelia burgdorferi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14383-14388(1997).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=11121028; DOI=10.1073/pnas.97.26.14224;
RA   Soell D., Becker H.D., Plateau P., Blanquet S., Ibba M.;
RT   "Context-dependent anticodon recognition by class I lysyl-tRNA
RT   synthetases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14224-14228(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC         tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC         COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Able to charge E.coli tRNA(Lys) in vitro.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000783; AAC67006.1; -; Genomic_DNA.
DR   PIR; B70182; B70182.
DR   RefSeq; NP_212793.1; NC_001318.1.
DR   RefSeq; WP_002663481.1; NC_001318.1.
DR   AlphaFoldDB; O51603; -.
DR   SMR; O51603; -.
DR   STRING; 224326.BB_0659; -.
DR   PRIDE; O51603; -.
DR   EnsemblBacteria; AAC67006; AAC67006; BB_0659.
DR   KEGG; bbu:BB_0659; -.
DR   PATRIC; fig|224326.49.peg.1050; -.
DR   HOGENOM; CLU_025562_1_0_12; -.
DR   OMA; DWPMRWA; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 6.10.20.10; -; 1.
DR   HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR002904; Lys-tRNA-ligase.
DR   InterPro; IPR042078; Lys-tRNA-ligase_SC_fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR37940; PTHR37940; 1.
DR   Pfam; PF01921; tRNA-synt_1f; 1.
DR   SUPFAM; SSF48163; SSF48163; 1.
DR   TIGRFAMs; TIGR00467; lysS_arch; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..521
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152736"
FT   MOTIF           32..40
FT                   /note="'HIGH' region"
FT   MOTIF           280..284
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   521 AA;  60938 MW;  6AF5A461AED3251D CRC64;
     MKTAHWADFY AEKIKKEKGP KNLYTVASGI TPSGTVHIGN FREVISVDLV ARALRDSGSK
     VRFIYSWDNY DVFRKVPKNM PEQELLTTYL RQAITRVPDT RSHKTSYARA NEIEFEKYLP
     VVGINPEFID QSKQYTSNAY ASQIKFALDH KKELSEALNE YRTSKLEENW YPISVFCTKC
     NRDTTTVNNY DNHYSVEYSC ECGNQESLDI RTTWAIKLPW RIDWPMRWKY EKVDFEPAGK
     DHHSSGGSFD TSKNIVKIFQ GSPPVTFQYD FISIKGRGGK ISSSSGDVIS LKDVLEVYTP
     EVTRFLFAAT KPNTEFSISF DLDVIKIYED YDKFERIYYG VEDVKEEKKR AFKRIYELSQ
     PYMPSKRIPY QVGFRHLSVI SQIFENNINK ILNYLKNVQE DQKDKLINKI NCAINWIRDF
     APEDFKFSLR SKFDNMEILE ENSKKAINEL LDFLKKNFEV ATEQDIQNEI YKISRENNIE
     PALFFKQIYK ILIDKEKGPK LAGFIKIIGI DRFEKITSKY V