ID   TILS_MANSM              Reviewed;         426 AA.
AC   Q65UE9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=MS0804;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU37411.1; -; Genomic_DNA.
DR   RefSeq; WP_011199983.1; NC_006300.1.
DR   AlphaFoldDB; Q65UE9; -.
DR   SMR; Q65UE9; -.
DR   STRING; 221988.MS0804; -.
DR   EnsemblBacteria; AAU37411; AAU37411; MS0804.
DR   KEGG; msu:MS0804; -.
DR   eggNOG; COG0037; Bacteria.
DR   HOGENOM; CLU_018869_2_0_6; -.
DR   OMA; QTETFFL; -.
DR   OrthoDB; 666797at2; -.
DR   Proteomes; UP000000607; 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; 1.
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; tRNA processing.
FT   CHAIN           1..426
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_0000181719"
FT   BINDING         22..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   426 AA;  49558 MW;  CE37F04B0EA62B43 CRC64;
     MSDIFNQFQQ QIYQQKILIA FSGGLDSTAL LALCKKLQEN RPHFQFRAIH IHHGLSPNAD
     KWALHCENIC RQFSIPLIVE KVRVDKSNGI EAGAREARYH AIANHLNIDE VLATAHHLND
     QTETFLLALK RGSGVQGLSA MQKESVVFNL PIFRPLLQFT RAQLEDYVKS QKINWIEDES
     NEDNSYDRNF LRNIILPKMK TRWAHFDQAV YRAAQHCFEQ TQLVNELLED EFQKIFEKND
     RTLSVKLFDR YSYIKQKALL RLWLARLQLA MPSQKQLEQL IRDVIFAKPD AIPQFKLANQ
     VIRRYQQKLY LTADFADLTD VAVPLKISQT VPLPDGLGHI SLREQSGCFV FSWRHYQVQL
     PPCKQPIEIR FAYSGKVKLH KNGVNQDIKK VWQNLNVPPW LRNRTPLIFY GDQLKSAVGF
     FKVFDC