ID   SYK_BORGP               Reviewed;         521 AA.
AC   Q937U7; Q660L1;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; Synonyms=lysK;
GN   OrderedLocusNames=BG0682;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DK6;
RA   Ibba M.;
RT   "Differentiation of Borrelia burgdorferi sensu lato strains using class I
RT   lysyl-tRNA synthetase encoding genes.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(2004).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00177}.
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DR   EMBL; AJ416852; CAC95161.1; -; Genomic_DNA.
DR   EMBL; CP000013; AAU07510.1; -; Genomic_DNA.
DR   RefSeq; WP_011193965.1; NZ_CP028872.1.
DR   AlphaFoldDB; Q937U7; -.
DR   SMR; Q937U7; -.
DR   STRING; 290434.BG0682; -.
DR   EnsemblBacteria; AAU07510; AAU07510; BG0682.
DR   KEGG; bga:BG0682; -.
DR   eggNOG; COG1384; Bacteria.
DR   HOGENOM; CLU_025562_1_0_12; -.
DR   OMA; DWPMRWA; -.
DR   OrthoDB; 256927at2; -.
DR   Proteomes; UP000002276; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..521
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152737"
FT   MOTIF           32..40
FT                   /note="'HIGH' region"
FT   MOTIF           280..284
FT                   /note="'KMSKS' region"
FT   CONFLICT        297
FT                   /note="I -> V (in Ref. 1; CAC95161)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   521 AA;  61035 MW;  BE8434771D84220E CRC64;
     MKTAHWADFY AEKIKKEKGP KNIYTVASGI TPSGTVHIGN FREVISVDLV ARALKDSGSQ
     VRFIYSWDNY DVFRKVPKNM PEQELLTTYL RQAITRVPDT RGYKTSYARA NEIEFEKYLP
     IVGINPEFID QSKKYTNSTY ASQIKFALNH KKELAEALNE YRTSKLEENW YPISIFCTKC
     NRDTTTVNNY DNHYSVKYSC ECGNQESLDI RTTWAIKLPW RIDWPMRWKY EKVDFEPAGK
     DHHSSGGSFD TSKNIVKIFQ GSPPVTFQYD FISIKGRGGK ISSSLGDVIS LKDVLEIYTP
     EVTRFLFAAT KPNTEFSISF DLDVIKIYED YDRFERIYYG VEDIKEEKKR SFKRIYELSQ
     PYMPSKRIPY QIGFRHLSVI CQIFENNINK ILNYLKNVQD DQKDKLINKI KCVINWIKDF
     APEDFKFLLR SKFDNIEILK EDNKKAISEL LDSLKKNFEV ATEQDIQNEI YKISRENNIE
     PALFFKQIYK ILIDKEKGPK LAGFIKIIGI DRFEKIVSKY I