ID   TILS_HELMO              Reviewed;         470 AA.
AC   Q9ZGE2; Q8GDP5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 82.
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};
OS   Heliobacterium mobile (Heliobacillus mobilis).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliobacterium.
OX   NCBI_TaxID=28064;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9843979; DOI=10.1073/pnas.95.25.14851;
RA   Xiong J., Inoue K., Bauer C.E.;
RT   "Tracking molecular evolution of photosynthesis by characterization of a
RT   major photosynthesis gene cluster from Heliobacillus mobilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:14851-14856(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12446909; DOI=10.1126/science.1075558;
RA   Raymond J., Zhaxybayeva O., Gogarten J.P., Gerdes S.Y., Blankenship R.E.;
RT   "Whole-genome analysis of photosynthetic prokaryotes.";
RL   Science 298:1616-1620(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Liolios K.G., Chu L., Ostrovskaya O., Mendybaeva N., Koukharenko V.,
RA   Gerdes S., Kyrpides N., Overbeek R.;
RL   Submitted (AUG-2002) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN87535.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF080002; AAC84036.1; -; Genomic_DNA.
DR   EMBL; AY142931; AAN87535.1; ALT_FRAME; Genomic_DNA.
DR   PIR; T31465; T31465.
DR   AlphaFoldDB; Q9ZGE2; -.
DR   SMR; Q9ZGE2; -.
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; 1.
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..470
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_0000181703"
FT   BINDING         29..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   470 AA;  53601 MW;  C2B548326258E169 CRC64;
     MNHLLQRFSQ SLCRLGINKP RERIVIALSG GADSVCLLLL FKKVSPQFGI ELAAAHYNHG
     MRGKESDEDA AFVAELTNRL QVPLFLETAP LKWWQQEPGT KMEAARRLRY DFLSRSAEQA
     GARWIALAHH ADDMAETVLF HMLRGSGIKG LSGIPAKRGP FVRPLLPFRR KELEEFLKAE
     GQHWRHDSSN DSDVYTRNRI RHQIMPALLS FNPKLVETLC RNADLLRADA EFLDRECELV
     YGQVQQEEGL KVQALVDLPL ALRRRVLRRF LEPENPGSEK TDAILEQLQK NFGRSKIVDQ
     VGGKYLINEG GILRSYEELP WLENQDFFYP IAIPKEKNHS VRLEVPEAEG SLEVTLSTKK
     PVSLMHDEGP PSKPMKTALQ LKAEVLQRGP LSIRNRRPGD WLSLAGRAGR KKLKEFFIDK
     KIPRQLRDRI PLLTSGEEVL WVIGCWTGCH DTIDQPGQDV ITFQWYGKTI