ID   TATD_CROTZ              Reviewed;         263 AA.
AC   C9XTA5;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 64.
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=Ctu_02700;
OS   Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX   PubMed=21037008; DOI=10.1128/jb.01162-10;
RA   Stephan R., Lehner A., Tischler P., Rattei T.;
RT   "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT   pathogen causing deaths in neonates.";
RL   J. Bacteriol. 193:309-310(2011).
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=CBA27123.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FN543093; CBA27123.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C9XTA5; -.
DR   SMR; C9XTA5; -.
DR   EnsemblBacteria; CBA27123; CBA27123; CTU_02700.
DR   KEGG; ctu:CTU_02700; -.
DR   PATRIC; fig|693216.3.peg.259; -.
DR   HOGENOM; CLU_031506_1_2_6; -.
DR   Proteomes; UP000002069; 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; 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; PS01091; TATD_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
FT   CHAIN           1..263
FT                   /note="3'-5' ssDNA/RNA exonuclease TatD"
FT                   /id="PRO_0000412732"
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   263 AA;  29148 MW;  577560317E335CC0 CRC64;
     MFDIGLNITS SQFDHDRDEM IARARAAGVD SMLFTGTSLE ESDRACAFAR RYAGCWSTAG
     VHPHDASTWN DESAARLRAL ASEPEVVAIG ECGLDFNRNF STPAEQEHAF TEQLRLAAAL
     ALPVFLHCRD AHARFLALLD PWLDKLPGAV LHCFTGTEQE ARECLARGMY LGITGWVCDE
     RRGLELRALL PIIPADRLLL ETDAPYLLPR DLTPKPASRR NEPCWLPHIL TQVAQWRGED
     PAWLEAATDA NAARLFLKNA SPA