TSAE_ECOLI
ID TSAE_ECOLI Reviewed; 153 AA.
AC P0AF67; P31805; Q2M6D7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE;
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE;
GN Name=tsaE; Synonyms=yjeE; OrderedLocusNames=b4168, JW4126;
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;
RX PubMed=7511774; DOI=10.1111/j.1365-2958.1994.tb00300.x;
RA Tsui H.-C.T., Zhao G., Feng G., Leung H.-C.E., Winkler M.E.;
RT "The mutL repair gene of Escherichia coli K-12 forms a superoperon with a
RT gene encoding a new cell-wall amidase.";
RL Mol. Microbiol. 11:189-202(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
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 [4]
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 [5]
RP ATPASE ACTIVITY, KINETIC PARAMETERS, DISRUPTION PHENOTYPE, SUBUNIT,
RP INTERACTION WITH TSAB, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=19376873; DOI=10.1128/jb.00136-09;
RA Handford J.I., Ize B., Buchanan G., Butland G.P., Greenblatt J., Emili A.,
RA Palmer T.;
RT "Conserved network of proteins essential for bacterial viability.";
RL J. Bacteriol. 191:4732-4749(2009).
RN [6]
RP FUNCTION IN T(6)A37 FORMATION, GENE NAME, AND INTERACTION WITH TSAB.
RC STRAIN=K12;
RX PubMed=22378793; DOI=10.1074/jbc.m112.344028;
RA Deutsch C., El Yacoubi B., de Crecy-Lagard V., Iwata-Reuyl D.;
RT "Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA
RT nucleoside.";
RL J. Biol. Chem. 287:13666-13673(2012).
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC with adenine. Is probably involved in the transfer of the
CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC group of A37, together with TsaD and TsaB. TsaE seems to play an
CC indirect role in the t(6)A biosynthesis pathway, possibly in regulating
CC the core enzymatic function of TsaD. Displays ATPase activity in vitro.
CC {ECO:0000269|PubMed:22378793}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=169 uM for ATP {ECO:0000269|PubMed:19376873};
CC Note=kcat is 0.0026 sec(-1) for ATP hydrolysis.;
CC -!- SUBUNIT: Homodimer. Interacts with TsaB. {ECO:0000269|PubMed:19376873,
CC ECO:0000269|PubMed:22378793}.
CC -!- INTERACTION:
CC P0AF67; P63177: rlmB; NbExp=3; IntAct=EBI-561268, EBI-562712;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19376873}.
CC -!- DISRUPTION PHENOTYPE: Appears essential for growth, since no null
CC mutants can be obtained. Conditional depletion of this gene leads to
CC very elongated cells, 1.5 to 1.75 times wider than wild-type,
CC displaying an unusual distribution of the DNA, which appears to be
CC located around the periphery of the cell rather than throughout the
CC cytoplasm. The TsaE depletion phenotype is suppressed by overexpressing
CC the response regulator RstA. {ECO:0000269|PubMed:19376873}.
CC -!- MISCELLANEOUS: TsaBCDE are necessary and sufficient for tRNA(NNU)
CC t(6)A37 threonylcarbamoyladenosine modification in vitro in E.coli.
CC {ECO:0000305|PubMed:22378793}.
CC -!- SIMILARITY: Belongs to the TsaE family. {ECO:0000305}.
CC -!- CAUTION: The well-known t(6)A modification appears to be a hydrolyzed
CC artifact of natural cyclic t(6)A (ct(6)A) that occurs during the
CC preparation and handling of tRNA in E.coli and many other species
CC (PubMed:23242255). In these species, the t(6)A modification is
CC processed further by dehydration into ct(6)A, a reaction catalyzed by
CC TcdA. {ECO:0000305}.
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DR EMBL; L19346; AAA20096.1; -; Unassigned_DNA.
DR EMBL; U14003; AAA97064.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77125.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78169.1; -; Genomic_DNA.
DR PIR; S56393; S56393.
DR RefSeq; NP_418589.1; NC_000913.3.
DR RefSeq; WP_000981977.1; NZ_STEB01000013.1.
DR AlphaFoldDB; P0AF67; -.
DR SMR; P0AF67; -.
DR BioGRID; 4262705; 155.
DR BioGRID; 852976; 1.
DR ComplexPortal; CPX-1094; YgjD-YeaZ-YjeE complex.
DR DIP; DIP-47867N; -.
DR IntAct; P0AF67; 23.
DR STRING; 511145.b4168; -.
DR ChEMBL; CHEMBL3309030; -.
DR jPOST; P0AF67; -.
DR PaxDb; P0AF67; -.
DR PRIDE; P0AF67; -.
DR EnsemblBacteria; AAC77125; AAC77125; b4168.
DR EnsemblBacteria; BAE78169; BAE78169; BAE78169.
DR GeneID; 60902986; -.
DR GeneID; 948684; -.
DR KEGG; ecj:JW4126; -.
DR KEGG; eco:b4168; -.
DR PATRIC; fig|1411691.4.peg.2533; -.
DR EchoBASE; EB1707; -.
DR eggNOG; COG0802; Bacteria.
DR HOGENOM; CLU_087829_2_2_6; -.
DR InParanoid; P0AF67; -.
DR OMA; FTDDAIC; -.
DR PhylomeDB; P0AF67; -.
DR BioCyc; EcoCyc:EG11757-MON; -.
DR BioCyc; MetaCyc:EG11757-MON; -.
DR PRO; PR:P0AF67; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000408; C:EKC/KEOPS complex; IPI:ComplexPortal.
DR GO; GO:0043531; F:ADP binding; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:EcoCyc.
DR GO; GO:1990145; P:maintenance of translational fidelity; IC:ComplexPortal.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:ComplexPortal.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003442; T6A_TsaE.
DR Pfam; PF02367; TsaE; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00150; T6A_YjeE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; tRNA processing.
FT CHAIN 1..153
FT /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT TsaE"
FT /id="PRO_0000096205"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 38..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 153 AA; 16853 MW; 49F8C7AA5965EC55 CRC64;
MMNRVIPLPD EQATLDLGER VAKACDGATV IYLYGDLGAG KTTFSRGFLQ ALGHQGNVKS
PTYTLVEPYT LDNLMVYHFD LYRLADPEEL EFMGIRDYFA NDAICLVEWP QQGTGVLPDP
DVEIHIDYQA QGREARVSAV SSAGELLLAR LAG
