TILS_ECOLI
ID TILS_ECOLI Reviewed; 432 AA.
AC P52097;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=tRNA(Ile)-lysidine synthase;
DE EC=6.3.4.19;
DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase;
DE AltName: Full=tRNA(Ile)-lysidine synthetase;
GN Name=tilS; Synonyms=mesJ, yaeN; OrderedLocusNames=b0188, JW0183;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Yamamoto Y.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=9723924; DOI=10.1046/j.1365-2958.1998.00981.x;
RA Pichoff S., Alibaud L., Guedant A., Castanie M.-P., Bouche J.-P.;
RT "An Escherichia coli gene (yaeO) suppresses temperature-sensitive mutations
RT in essential genes by modulating Rho-dependent transcription termination.";
RL Mol. Microbiol. 29:859-869(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
RP CHARACTERIZATION.
RX PubMed=14527414; DOI=10.1016/s1097-2765(03)00346-0;
RA Soma A., Ikeuchi Y., Kanemasa S., Kobayashi K., Ogasawara N., Ote T.,
RA Kato J., Watanabe K., Sekine Y., Suzuki T.;
RT "An RNA-modifying enzyme that governs both the codon and amino acid
RT specificities of isoleucine tRNA.";
RL Mol. Cell 12:689-698(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RA Gu M., Burling T., Lima C.D.;
RT "Structure of the MesJ Pp-ATPase from Escherichia coli.";
RL Submitted (JAN-2003) to the PDB data bank.
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 This enzyme is essential for viability.
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;
CC Evidence={ECO:0000269|PubMed:14527414};
CC -!- INTERACTION:
CC P52097; P52097: tilS; NbExp=3; IntAct=EBI-556745, EBI-556745;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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:0000305}.
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DR EMBL; D49445; BAA08428.1; -; Genomic_DNA.
DR EMBL; Z50870; CAA90751.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08617.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73299.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77863.1; -; Genomic_DNA.
DR EMBL; BR000032; FAA00003.1; -; Genomic_DNA.
DR PIR; D64743; D64743.
DR RefSeq; NP_414730.1; NC_000913.3.
DR RefSeq; WP_000176549.1; NZ_SSZK01000004.1.
DR PDB; 1NI5; X-ray; 2.65 A; A=1-432.
DR PDBsum; 1NI5; -.
DR AlphaFoldDB; P52097; -.
DR SMR; P52097; -.
DR BioGRID; 4261685; 173.
DR BioGRID; 849289; 3.
DR DIP; DIP-10190N; -.
DR IntAct; P52097; 17.
DR STRING; 511145.b0188; -.
DR ChEMBL; CHEMBL3309031; -.
DR jPOST; P52097; -.
DR PaxDb; P52097; -.
DR PRIDE; P52097; -.
DR EnsemblBacteria; AAC73299; AAC73299; b0188.
DR EnsemblBacteria; BAA77863; BAA77863; BAA77863.
DR GeneID; 944889; -.
DR KEGG; ecj:JW0183; -.
DR KEGG; eco:b0188; -.
DR PATRIC; fig|1411691.4.peg.2091; -.
DR EchoBASE; EB3011; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_018869_2_0_6; -.
DR InParanoid; P52097; -.
DR OMA; QTETFFL; -.
DR PhylomeDB; P52097; -.
DR BioCyc; EcoCyc:G6096-MON; -.
DR BioCyc; MetaCyc:G6096-MON; -.
DR BRENDA; 6.3.4.19; 2026.
DR EvolutionaryTrace; P52097; -.
DR PRO; PR:P52097; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0032267; F:tRNA(Ile)-lysidine synthase activity; IDA:EcoCyc.
DR GO; GO:0006400; P:tRNA modification; IDA:EcoliWiki.
DR GO; GO:0002136; P:tRNA wobble base lysidine biosynthesis; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Reference proteome; tRNA processing.
FT CHAIN 1..432
FT /note="tRNA(Ile)-lysidine synthase"
FT /id="PRO_0000181689"
FT BINDING 20..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 1..9
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1NI5"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:1NI5"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 205..234
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:1NI5"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 298..311
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1NI5"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:1NI5"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:1NI5"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1NI5"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:1NI5"
SQ SEQUENCE 432 AA; 48204 MW; 26946DC7220B5A40 CRC64;
MTLTLNRQLL TSRQILVAFS GGLDSTVLLH QLVQWRTENP GVALRAIHVH HGLSANADAW
VTHCENVCQQ WQVPLVVERV QLAQEGLGIE AQARQARYQA FARTLLPGEV LVTAQHLDDQ
CETFLLALKR GSGPAGLSAM AEVSEFAGTR LIRPLLARTR GELVQWARQY DLRWIEDESN
QDDSYDRNFL RLRVVPLLQQ RWPHFAEATA RSAALCAEQE SLLDELLADD LAHCQSPQGT
LQIVPMLAMS DARRAAIIRR WLAGQNAPMP SRDALVRIWQ EVALAREDAS PCLRLGAFEI
RRYQSQLWWI KSVTGQSENI VPWQTWLQPL ELPAGLGSVQ LNAGGDIRPP RADEAVSVRF
KAPGLLHIVG RNGGRKLKKI WQELGVPPWL RDTTPLLFYG ETLIAAAGVF VTQEGVAEGE
NGVSFVWQKT LS
