TATD_KLEP3
ID TATD_KLEP3 Reviewed; 263 AA.
AC B5XYH5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=KPK_5337;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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}.
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DR EMBL; CP000964; ACI10303.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XYH5; -.
DR SMR; B5XYH5; -.
DR EnsemblBacteria; ACI10303; ACI10303; KPK_5337.
DR KEGG; kpe:KPK_5337; -.
DR HOGENOM; CLU_031506_1_2_6; -.
DR OMA; NEPCALP; -.
DR OrthoDB; 915852at2; -.
DR Proteomes; UP000001734; 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; 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..263
FT /note="3'-5' ssDNA/RNA exonuclease TatD"
FT /id="PRO_0000412744"
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; 28980 MW; 925259D30BEB5420 CRC64;
MFDIGVNLTS SQFSRDHDEV VARARAAGVH GMLLTGTNLP ESQQAQRMAS HYSGCWSTAG
VHPHDGSSWS PAVAEAIYTL AREPQVVAIG ECGLDFNRNF STPQEQEAAF SAQLALAAEL
AMPVFLHCRD AHDRFLALLK PWLEKIPGAV LHCFTGSRSE VQECLDLGLF IGITGWVCDE
RRGLELRELL PAIPAERLLL ETDAPYLLPR DLKPRPASRR NEPAYLPHIL ASVASWRGEE
TQWLEAQTDA NVRTLFGIDV NGV