ID   TILS_LACLA              Reviewed;         423 AA.
AC   Q9CJH4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=LL0019;
GN   ORFNames=L1002;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK04117.1; -; Genomic_DNA.
DR   PIR; C86627; C86627.
DR   RefSeq; NP_266175.1; NC_002662.1.
DR   RefSeq; WP_010905037.1; NC_002662.1.
DR   AlphaFoldDB; Q9CJH4; -.
DR   SMR; Q9CJH4; -.
DR   STRING; 272623.L1002; -.
DR   PaxDb; Q9CJH4; -.
DR   PRIDE; Q9CJH4; -.
DR   EnsemblBacteria; AAK04117; AAK04117; L1002.
DR   KEGG; lla:L1002; -.
DR   PATRIC; fig|272623.7.peg.21; -.
DR   eggNOG; COG0037; Bacteria.
DR   HOGENOM; CLU_018869_0_2_9; -.
DR   OMA; NRIRNHY; -.
DR   Proteomes; UP000002196; 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   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; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..423
FT                   /note="tRNA(Ile)-lysidine synthase"
FT                   /id="PRO_0000181708"
FT   BINDING         29..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   423 AA;  49574 MW;  6C7D09EFD72584CD CRC64;
     MTPAQRKFLK IVKDEHYFDK DSKILLALSG GKDSMTLFNW LYDLKEVLGI ELGLAHINHG
     LREESKFEEI ALREMATKLK VPIYVDKFTG EFTEKNARDF RYQFFEKLMI GENYNILLTA
     HHQGDLVETV LMRQITGRPL RSLQGIADRQ PFAGGQLIRP LLKFTKEELD AQTYYEDSTN
     QGLDYFRNRI RNQLIPELKK ENPQFSQSIS DLSSEIKKAL AVINQKISEL EIVDEKISSK
     KFISQTKELQ HFILQAFFAQ YPEIEVSKKK FAELLHIINR PQQYFAKLNK EFYFVKTKDF
     FYLEKIQLER ENSVEIVSEN PQDESFMEVY LPLEGEIEIR KRQPGDQILI NGHHKKLRKF
     FIDNKVPLKA RENPLIFVDK KLYAIVGLAC SDLSKMLKND KIRRILWVKP SIGEEINDAR
     KKS