ID   TILS_BART1              Reviewed;         495 AA.
AC   A9IYI2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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}; OrderedLocusNames=BT_2359;
OS   Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105476 / IBS 506;
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems as
RT   host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
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; AM260525; CAK02367.1; -; Genomic_DNA.
DR   RefSeq; WP_012232425.1; NC_010161.1.
DR   AlphaFoldDB; A9IYI2; -.
DR   SMR; A9IYI2; -.
DR   STRING; 382640.BT_2359; -.
DR   EnsemblBacteria; CAK02367; CAK02367; BT_2359.
DR   KEGG; btr:BT_2359; -.
DR   eggNOG; COG0037; Bacteria.
DR   HOGENOM; CLU_018869_3_3_5; -.
DR   OMA; YKRTLYR; -.
DR   OrthoDB; 666797at2; -.
DR   Proteomes; UP000001592; 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; 2.
DR   TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; tRNA processing.
FT   CHAIN           1..495
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_1000085361"
FT   BINDING         26..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   495 AA;  56499 MW;  1AF0F09C61C85825 CRC64;
     MCVRLARNLF KTSDFIPCRR VILAVSGGSD SLALMFLVKE YLETLLIPPE IIAVTVDHQL
     RKESAREAEI VAEICRDHHI KHITVRWEGK KPKTHLAFSA RIARYDLLVQ EAQKQGASLI
     MTGHTLNDQV ETYQMRCQRL QKRRGALRDE VGAMCDGGAA SGFAGALRDK AGARRDEDYV
     RETRKNIAEK SYGVLYERGL SCIPREALLH RKVRLIRPLL GVQRQTLRNY LRLQGKTWID
     DPTNEDRNFE RVRVRQSLSS QKLVNIAQKI NKAAWQRRQQ AQNIADLILA LDITVQYGRC
     FIVKPAPFLQ KHSCFPFVVG LFAVLMGGGF YLLSNQKLSM LVQKLCLNSP EKRRFTCAGC
     VIEYNKEGIA LWRERRNMKE ALVEPDETLL WDGRYRITNH GSEAIKVGVA NLEQLKSLLQ
     NSNSNLEKPH FPSLQSLLML SNDKGCDIPE LISQAIIHKN VIIKRIMAPF DWLSSREDAA
     LVNVVEPFFN LEVKR