ID   TILS_BUCAI              Reviewed;         440 AA.
AC   P57211;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
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}; Synonyms=mesJ;
GN   OrderedLocusNames=BU110;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(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; BA000003; BAB12829.1; -; Genomic_DNA.
DR   RefSeq; NP_239943.1; NC_002528.1.
DR   RefSeq; WP_010895950.1; NC_002528.1.
DR   AlphaFoldDB; P57211; -.
DR   SMR; P57211; -.
DR   STRING; 107806.10038794; -.
DR   EnsemblBacteria; BAB12829; BAB12829; BAB12829.
DR   KEGG; buc:BU110; -.
DR   PATRIC; fig|107806.10.peg.118; -.
DR   eggNOG; COG0037; Bacteria.
DR   HOGENOM; CLU_018869_2_0_6; -.
DR   OMA; QTETFFL; -.
DR   Proteomes; UP000001806; 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; 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   InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd.
DR   PANTHER; PTHR43033; PTHR43033; 2.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF09179; TilS; 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; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..440
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_0000181664"
FT   BINDING         19..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   440 AA;  52630 MW;  46547AC01B27782E CRC64;
     MIKEIISQYQ NKSFLVAYSG GLDSTVLLYK LLEIKKKYYI KIRAIHINHN LTLLSKKWSE
     HCKKICNINH IPLIVENINI KNKTNNLEEK LRIKRYNIIY NHLFSDEILL TGHHINDQCE
     TFFLSLKRGS GPTGLSSMSF ETLFGTKKIV RPFLKKTKIE LQTWAKKKKL HWIEDFSNLN
     IDYDRNFIRN EVIPILEKRW SYFLKNCFRT TIICQQETRL LNDFLRERIY KLIKFDDSLN
     IENFKNIKQA MCTALIRYWL LLKKIKMPSY KNIQCIYRQM IFSRIDSNPK IILGKHEVRR
     YKQSLHFIKT QPSLKNTLLF WHKNNIKLTL PNNLGYLIKN NNGTVLPGPK ENELINIRFQ
     YEGYVLILGR SKKRKIKKIW QEKNIPPWLR NQIPLLFYNN YFISAIGVFV VNIKNKNRTK
     CIISWQNDLK STTNNFFSFY