ID   TILS_WOLSU              Reviewed;         326 AA.
AC   Q7MR31; Q9ZEN6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=WS1770;
OS   Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS   11488 / FDC 602W) (Vibrio succinogenes).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=273121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC   11488 / FDC 602W;
RX   PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-210.
RX   PubMed=11004174; DOI=10.1128/jb.182.20.5757-5764.2000;
RA   Ullmann R., Gross R., Simon J., Unden G., Kroeger A.;
RT   "Transport of C4-dicarboxylates in Wolinella succinogenes.";
RL   J. Bacteriol. 182:5757-5764(2000).
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; BX571661; CAE10792.1; -; Genomic_DNA.
DR   EMBL; AJ131242; CAA10333.1; -; Genomic_DNA.
DR   RefSeq; WP_011139575.1; NC_005090.1.
DR   AlphaFoldDB; Q7MR31; -.
DR   SMR; Q7MR31; -.
DR   STRING; 273121.WS1770; -.
DR   EnsemblBacteria; CAE10792; CAE10792; WS1770.
DR   KEGG; wsu:WS1770; -.
DR   eggNOG; COG0037; Bacteria.
DR   HOGENOM; CLU_053500_0_0_7; -.
DR   OMA; LEWFLMQ; -.
DR   OrthoDB; 666797at2; -.
DR   Proteomes; UP000000422; 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; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..326
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_0000181806"
FT   BINDING         23..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
FT   CONFLICT        197
FT                   /note="K -> Q (in Ref. 2; CAA10333)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   326 AA;  38155 MW;  C2463ECD93D9DAFF CRC64;
     MGKIIQLQEE ERLRQGKNLL GFSGGVDSTA LFFLLLEREI PFDIALVNYH QRAQAKEEES
     YAKELAHRHQ KRCFTLSCPL GPSNFEHQAR LERYRFFESL IHQEGYARLL LAHHLGDRLE
     WLLMRLAQGS SLSTLLGFSS REIRLGYELI RPLGEITKEA LYDYLHQHQI RYFEDESNRD
     PKPLRNRFRP LSETLLKEHA QGLLQSFRFL QEEREILYGE DPRIRRDSLF YFPSQERETQ
     NLHLIDLSLK ALGYVMSQGE RQELLKSGFC VVLKGKVAIG RSERGIFIAP FERVIIPKAQ
     RERLRIAKIP PKVRPYCFMA GIDSLL