ID   TILS_BORAP              Reviewed;         440 AA.
AC   Q0SM64; G0IRX0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE            EC=6.3.4.19 {ECO:0000255|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000255|HAMAP-Rule:MF_01161};
GN   Name=tilS {ECO:0000255|HAMAP-Rule:MF_01161};
GN   OrderedLocusNames=BAPKO_0840, BafPKo_0816;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
CC   -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 of
CC       the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC       ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC       the amino acid specificity of the tRNA from methionine to isoleucine.
CC       {ECO:0000255|HAMAP-Rule:MF_01161}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC         diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC         Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC         ChEBI:CHEBI:456215; EC=6.3.4.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01161};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01161}.
CC   -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC       motif, predicted to be a P-loop motif involved in ATP binding.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01161}.
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DR   EMBL; CP000395; ABH02064.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL70005.1; -; Genomic_DNA.
DR   RefSeq; WP_011601226.1; NC_017238.1.
DR   AlphaFoldDB; Q0SM64; -.
DR   SMR; Q0SM64; -.
DR   STRING; 390236.BafPKo_0816; -.
DR   PRIDE; Q0SM64; -.
DR   EnsemblBacteria; AEL70005; AEL70005; BafPKo_0816.
DR   KEGG; baf:BAPKO_0840; -.
DR   KEGG; bafz:BafPKo_0816; -.
DR   PATRIC; fig|390236.22.peg.777; -.
DR   eggNOG; COG0037; Bacteria.
DR   HOGENOM; CLU_050646_0_0_12; -.
DR   OMA; SEEMRRP; -.
DR   OrthoDB; 666797at2; -.
DR   Proteomes; UP000005216; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01992; PP-ATPase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR012094; tRNA_Ile_lys_synt.
DR   InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR   PANTHER; PTHR43033; PTHR43033; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; tRNA processing.
FT   CHAIN           1..440
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_1000065603"
FT   BINDING         31..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   440 AA;  51673 MW;  DB98B7086DBB4A85 CRC64;
     MHFLDDNIQI KIDKFYKKNS LNKNRVIVAF SGGADSTTLL LNLKYYLSNN IIAFYFAHFI
     RPDNEQNKEI EHVKGFCDLY NIALQIKKCD IDIKSESVRL GVSIEELARK CRYNALENAL
     KENDANYIAL AHNENDQIET IIMRFFQGSF LDGLAGIPSV NKNIIRPLLE VSRPEIENFL
     SLNNIRVFID STNSQNLYLR NKVRNNLLPS IEKIFKGYEK CLKRISEFSK EFVNYFEKDE
     FFPVEKGKYY YSFDLKAFLD FPKYLVFRLI FKILNSEGIV AKISYKALNE LFKIEIDRKK
     NNVLLKTNDF FLEKRHNKIN LIFKRDEKFY KPFDFILEVG KWHSLSLGKI LLKCLECNAA
     SVSRLKCCSY EFRYKFFKDK LKAKKFFSKF IRCNPIYLML LALDNRLIGI IDLNTLNLVW
     SEKSILKKIS ISLIGGLLKE