TATD_ENT38
ID TATD_ENT38 Reviewed; 260 AA.
AC A4WFX9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=3'-5' ssDNA/RNA exonuclease TatD {ECO:0000255|HAMAP-Rule:MF_00901};
DE EC=3.1.11.- {ECO:0000255|HAMAP-Rule:MF_00901};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_00901};
DE AltName: Full=DNase TatD {ECO:0000255|HAMAP-Rule:MF_00901};
GN Name=tatD {ECO:0000255|HAMAP-Rule:MF_00901}; OrderedLocusNames=Ent638_3954;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00901};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00901}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00901}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC TatD-type hydrolase family. TatD subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00901}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABP62609.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000653; ABP62609.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041689559.1; NC_009436.1.
DR AlphaFoldDB; A4WFX9; -.
DR SMR; A4WFX9; -.
DR STRING; 399742.Ent638_3954; -.
DR EnsemblBacteria; ABP62609; ABP62609; Ent638_3954.
DR KEGG; ent:Ent638_3954; -.
DR eggNOG; COG0084; Bacteria.
DR HOGENOM; CLU_031506_1_2_6; -.
DR OrthoDB; 915852at2; -.
DR Proteomes; UP000000230; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IEA:UniProtKB-UniRule.
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; IPR015991; Hydrolase_TatD-type.
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 TIGRFAMs; TIGR00010; TIGR00010; 1.
DR PROSITE; PS01090; TATD_2; 1.
DR PROSITE; PS01091; TATD_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT CHAIN 1..260
FT /note="3'-5' ssDNA/RNA exonuclease TatD"
FT /id="PRO_0000412738"
FT BINDING 91
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00901"
FT BINDING 127
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00901"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00901"
SQ SEQUENCE 260 AA; 29396 MW; AF8BBF63CAE52E43 CRC64;
MFDIGLNLTS PQFANDRDDV VARAFAAGVK GLLLTGTNLH ESEHAQQLAQ GYERCWSTAG
VHPHDSSQWT DESAETLYKL AKTEEVVAIG ECGLDFNRNF STPVEQEAAF TAQLAIAAEL
EMPVFMHCRD AHERFLTLLE PWRDKLPGAV LHCFTGSRQE AVECLNRGLY LGITGWVCDE
RRGLELRELL PVIPADRLLV ETDAPYLLPR DMKPKPASRR NEPAYLGHIV ERIAHWRGEE
RQRLDAQTDE NVRRLFGITF