TATD_ECOLI
ID TATD_ECOLI Reviewed; 260 AA.
AC P27859; P27860; P78128; P78129; Q2M8E4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=3'-5' ssDNA/RNA exonuclease TatD {ECO:0000255|HAMAP-Rule:MF_00901, ECO:0000305};
DE EC=3.1.11.- {ECO:0000255|HAMAP-Rule:MF_00901, ECO:0000305|PubMed:25114049};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_00901, ECO:0000305|PubMed:25114049};
DE AltName: Full=DNase TatD {ECO:0000255|HAMAP-Rule:MF_00901, ECO:0000305};
GN Name=tatD {ECO:0000255|HAMAP-Rule:MF_00901, ECO:0000303|PubMed:9649434};
GN Synonyms=mttC, yigW, yigX; OrderedLocusNames=b4483, JW5931;
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=5KC;
RX PubMed=1584020; DOI=10.1111/j.1365-2958.1992.tb02166.x;
RA Bailey M.J.A., Koronakis V., Schmoll T., Hughes C.;
RT "Escherichia coli HlyT protein, a transcriptional activator of haemolysin
RT synthesis and secretion, is encoded by the rfaH (sfrB) locus required for
RT expression of sex factor and lipopolysaccharide genes.";
RL Mol. Microbiol. 6:1003-1012(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RC STRAIN=K12;
RX PubMed=9649434; DOI=10.1093/emboj/17.13.3640;
RA Sargent F., Bogsch E.G., Stanley N.R., Wexler M., Robinson C., Berks B.C.,
RA Palmer T.;
RT "Overlapping functions of components of a bacterial Sec-independent protein
RT export pathway.";
RL EMBO J. 17:3640-3650(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [4]
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 [5]
RP SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
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 PROTEIN SEQUENCE OF 1-6, FUNCTION AS A DNASE, COFACTOR, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10747959; DOI=10.1074/jbc.m000800200;
RA Wexler M., Sargent F., Jack R.L., Stanley N.R., Bogsch E.G., Robinson C.,
RA Berks B.C., Palmer T.;
RT "TatD is a cytoplasmic protein with DNase activity. No requirement for TatD
RT family proteins in sec-independent protein export.";
RL J. Biol. Chem. 275:16717-16722(2000).
RN [8]
RP INDUCTION.
RX PubMed=11160116; DOI=10.1128/jb.183.5.1801-1804.2001;
RA Jack R.L., Sargent F., Berks B.C., Sawers G., Palmer T.;
RT "Constitutive expression of Escherichia coli tat genes indicates an
RT important role for the twin-arginine translocase during aerobic and
RT anaerobic growth.";
RL J. Bacteriol. 183:1801-1804(2001).
RN [9]
RP PROPOSED FUNCTION IN QUALITY CONTROL.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=19343049; DOI=10.1038/embor.2009.34;
RA Matos C.F., Di Cola A., Robinson C.;
RT "TatD is a central component of a Tat translocon-initiated quality control
RT system for exported FeS proteins in Escherichia coli.";
RL EMBO Rep. 10:474-479(2009).
RN [10]
RP RETRACTION NOTICE OF PUBMED:19343049, AND LACK OF FUNCTION IN QUALITY
RP CONTROL.
RX PubMed=20659466; DOI=10.1016/j.febslet.2010.07.039;
RA Lindenstrauss U., Matos C.F., Graubner W., Robinson C., Brueser T.;
RT "Malfolded recombinant Tat substrates are Tat-independently degraded in
RT Escherichia coli.";
RL FEBS Lett. 584:3644-3648(2010).
RN [11] {ECO:0007744|PDB:1XWY}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS, AND
RP SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of tatD DNase from Escherichia coli at 2.0 A
RT resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [12] {ECO:0007744|PDB:4P5U, ECO:0007744|PDB:4PE8}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF HIS-62; HIS-64; GLU-91; HIS-127; HIS-152; GLU-201 AND
RP ASP-203.
RC STRAIN=K12;
RX PubMed=25114049; DOI=10.1093/nar/gku732;
RA Chen Y.C., Li C.L., Hsiao Y.Y., Duh Y., Yuan H.S.;
RT "Structure and function of TatD exonuclease in DNA repair.";
RL Nucleic Acids Res. 42:10776-10785(2014).
CC -!- FUNCTION: 3'-5' exonuclease that prefers single-stranded DNA and RNA.
CC May play a role in the H(2)O(2)-induced DNA damage repair.
CC {ECO:0000255|HAMAP-Rule:MF_00901, ECO:0000269|PubMed:10747959,
CC ECO:0000269|PubMed:25114049}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00901,
CC ECO:0000269|PubMed:10747959, ECO:0000269|PubMed:25114049};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:25114049};
CC Note=No activity in the presence of Ca(2+) or Zn(2+).
CC {ECO:0000269|PubMed:25114049};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00901,
CC ECO:0000269|PubMed:10747959, ECO:0000269|PubMed:25114049,
CC ECO:0000269|Ref.11}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00901,
CC ECO:0000269|PubMed:10747959, ECO:0000269|PubMed:25114049}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:11160116}.
CC -!- DISRUPTION PHENOTYPE: Knockout cells are less resistant to the DNA
CC damaging agent H(2)O(2). {ECO:0000269|PubMed:25114049}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC TatD-type hydrolase family. TatD subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00901, ECO:0000305}.
CC -!- CAUTION: Was suggested to be a central component of a quality control
CC system that is linked to the Tat translocation system
CC (PubMed:19343049). However, it was shown later that malfolded Tat
CC substrates are Tat-independently degraded and that TatD is not involved
CC in quality control of the Tat substrates (PubMed:20659466).
CC {ECO:0000305|PubMed:19343049, ECO:0000305|PubMed:20659466}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA67636.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA67637.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA06727.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X65013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ005830; CAA06727.1; ALT_INIT; Genomic_DNA.
DR EMBL; M87049; AAA67636.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M87049; AAA67637.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48229.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77462.1; -; Genomic_DNA.
DR PIR; A65189; A65189.
DR RefSeq; WP_000459630.1; NZ_SSZK01000046.1.
DR RefSeq; YP_026271.1; NC_000913.3.
DR PDB; 1XWY; X-ray; 2.00 A; A=1-260.
DR PDB; 4P5U; X-ray; 2.00 A; A=1-260.
DR PDB; 4PE8; X-ray; 2.89 A; A=1-260.
DR PDBsum; 1XWY; -.
DR PDBsum; 4P5U; -.
DR PDBsum; 4PE8; -.
DR AlphaFoldDB; P27859; -.
DR SMR; P27859; -.
DR BioGRID; 4261335; 12.
DR STRING; 511145.b4483; -.
DR PaxDb; P27859; -.
DR PRIDE; P27859; -.
DR EnsemblBacteria; AAT48229; AAT48229; b4483.
DR EnsemblBacteria; BAE77462; BAE77462; BAE77462.
DR GeneID; 2847752; -.
DR KEGG; ecj:JW5931; -.
DR KEGG; eco:b4483; -.
DR PATRIC; fig|511145.12.peg.3955; -.
DR EchoBASE; EB1446; -.
DR eggNOG; COG0084; Bacteria.
DR HOGENOM; CLU_031506_1_2_6; -.
DR InParanoid; P27859; -.
DR OMA; PNEAPRI; -.
DR PhylomeDB; P27859; -.
DR BioCyc; EcoCyc:EG11481-MON; -.
DR BioCyc; MetaCyc:EG11481-MON; -.
DR EvolutionaryTrace; P27859; -.
DR PRO; PR:P27859; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:EcoCyc.
DR GO; GO:0004536; F:deoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoliWiki.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:EcoCyc.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:EcoCyc.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:EcoCyc.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:EcoCyc.
DR CDD; cd01310; TatD_DNAse; 1.
DR HAMAP; MF_00901; TatD_exonuclease; 1.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR024918; Exonuc_TatD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001130; TatD-like.
DR Pfam; PF01026; TatD_DNase; 1.
DR PIRSF; PIRSF005902; DNase_TatD; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01090; TATD_2; 1.
DR PROSITE; PS01091; TATD_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..260
FT /note="3'-5' ssDNA/RNA exonuclease TatD"
FT /id="PRO_0000201992"
FT BINDING 91
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7, ECO:0000255|HAMAP-
FT Rule:MF_00901"
FT BINDING 127
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7, ECO:0000255|HAMAP-
FT Rule:MF_00901"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7, ECO:0000255|HAMAP-
FT Rule:MF_00901"
FT MUTAGEN 62
FT /note="H->A: Significant decrease in nuclease activity."
FT /evidence="ECO:0000269|PubMed:25114049"
FT MUTAGEN 64
FT /note="H->A: No change in nuclease activity."
FT /evidence="ECO:0000269|PubMed:25114049"
FT MUTAGEN 91
FT /note="E->A: Lack of nuclease activity."
FT /evidence="ECO:0000269|PubMed:25114049"
FT MUTAGEN 127
FT /note="H->A: No change in nuclease activity."
FT /evidence="ECO:0000269|PubMed:25114049"
FT MUTAGEN 152
FT /note="H->A: No change in nuclease activity."
FT /evidence="ECO:0000269|PubMed:25114049"
FT MUTAGEN 201
FT /note="E->A: Lack of nuclease activity."
FT /evidence="ECO:0000269|PubMed:25114049"
FT MUTAGEN 203
FT /note="D->A: Lack of nuclease activity."
FT /evidence="ECO:0000269|PubMed:25114049"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1XWY"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:1XWY"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:1XWY"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:1XWY"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:1XWY"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1XWY"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4P5U"
FT HELIX 103..120
FT /evidence="ECO:0007829|PDB:1XWY"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:1XWY"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:1XWY"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1XWY"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1XWY"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:1XWY"
FT HELIX 241..256
FT /evidence="ECO:0007829|PDB:1XWY"
SQ SEQUENCE 260 AA; 28974 MW; C18FB5269849746F CRC64;
MFDIGVNLTS SQFAKDRDDV VACAFDAGVN GLLITGTNLR ESQQAQKLAR QYSSCWSTAG
VHPHDSSQWQ AATEEAIIEL AAQPEVVAIG ECGLDFNRNF STPEEQERAF VAQLRIAADL
NMPVFMHCRD AHERFMTLLE PWLDKLPGAV LHCFTGTREE MQACVAHGIY IGITGWVCDE
RRGLELRELL PLIPAEKLLI ETDAPYLLPR DLTPKPSSRR NEPAHLPHIL QRIAHWRGED
AAWLAATTDA NVKTLFGIAF
