ID   TILS_STRP4              Reviewed;         425 AA.
AC   B5E578;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=SPG_0011;
OS   Streptococcus pneumoniae serotype 19F (strain G54).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=512566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RX   PubMed=11442348; DOI=10.1089/10766290152044995;
RA   Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA   Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA   Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT   "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT   clinical isolate.";
RL   Microb. Drug Resist. 7:99-125(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RA   Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA   Tettelin H., Oggioni M.;
RT   "Pneumococcal beta glucoside metabolism investigated by whole genome
RT   comparison.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001015; ACF56646.1; -; Genomic_DNA.
DR   RefSeq; WP_001209049.1; NC_011072.1.
DR   AlphaFoldDB; B5E578; -.
DR   SMR; B5E578; -.
DR   KEGG; spx:SPG_0011; -.
DR   HOGENOM; CLU_018869_0_2_9; -.
DR   OMA; NRIRNHY; -.
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; IPR012796; Lysidine-tRNA-synth_C.
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; 2.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF11734; TilS_C; 1.
DR   SMART; SM00977; TilS_C; 1.
DR   TIGRFAMs; TIGR02433; lysidine_TilS_C; 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..425
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_1000137879"
FT   BINDING         27..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   425 AA;  49903 MW;  AD6284301B144B2A CRC64;
     MREQDFLNHF LKKGYFKKHA KAVLALSGGL DSMFLFKVLS TYQKELEIEL ILAHVNHKQR
     IESDWEEKEL RKLAAEAELP IYISNFSGEF SEARARNFRY DFFQEVMKKT GATALVTAHH
     ADDQVETILM RLIRGTRLRY LSGIKEKQVV GEIEIIRPFL HFQKKDFPSI FHFEDTSNQE
     NHYFRNRIRN SYLPELEKEN PRFRDAILGI GNEILDYDLA IAELSNNIDV ENLQQLFSYS
     ESTQRVLLQT YLNRFPDLNL TKAQFAEVQQ ILKSKSQYRH PIKNGYELIK EYQQFQICKI
     SPQADEKEDE LVLHYQNQVA YQGYLFSFGL PLEGELIQQI PVSRETSIHI RHRKTGDVLI
     QNGHRKKLRR LFIDLKIPME KRNSALIIEQ FGEIVSILGI ATNNLSKKTK NDIMNTVLYI
     EKIDR