UniProt functional annotation for P04995



	UniProt functional annotation for P04995

UniProt code: P04995.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Degrades single-stranded DNA (ssDNA) in a highly processive manner (PubMed:23609540). Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or AP lyase (PubMed:1329027). {ECO:0000269|PubMed:1329027, ECO:0000269|PubMed:23609540}.

Catalytic activity: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.1; Evidence={ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18219121, ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540}; Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000269|PubMed:18591666};

Activity regulation: Inhibited by 10 mM EDTA. {ECO:0000269|PubMed:23609540}.

Subunit: Monomer (PubMed:23609540). Interacts with ssb (via C- terminus); this interaction stimulates the exonuclease activity by recruiting the enzyme to its substrate (PubMed:18591666, PubMed:20018747). {ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540}.

Domain: The N-terminal exonuclease domain and the exonuclease C- terminal domain form a central positively charged groove which binds the DNA. {ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:23609540, ECO:0000305|PubMed:11101894, ECO:0000305|PubMed:18219121}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Degrades single-stranded DNA (ssDNA) in a highly processive manner (PubMed:23609540). Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or AP lyase (PubMed:1329027). {ECO:0000269\|PubMed:1329027, ECO:0000269\|PubMed:23609540}.


Catalytic activity:		Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.1; Evidence={ECO:0000269\|PubMed:18591666, ECO:0000269\|PubMed:20018747, ECO:0000269\|PubMed:23609540};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:18219121, ECO:0000269\|PubMed:18591666, ECO:0000269\|PubMed:20018747, ECO:0000269\|PubMed:23609540}; Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000269\|PubMed:18591666};
Activity regulation:		Inhibited by 10 mM EDTA. {ECO:0000269\|PubMed:23609540}.
Subunit:		Monomer (PubMed:23609540). Interacts with ssb (via C- terminus); this interaction stimulates the exonuclease activity by recruiting the enzyme to its substrate (PubMed:18591666, PubMed:20018747). {ECO:0000269\|PubMed:18591666, ECO:0000269\|PubMed:20018747, ECO:0000269\|PubMed:23609540}.
Domain:		The N-terminal exonuclease domain and the exonuclease C- terminal domain form a central positively charged groove which binds the DNA. {ECO:0000269\|PubMed:18591666, ECO:0000269\|PubMed:23609540, ECO:0000305\|PubMed:11101894, ECO:0000305\|PubMed:18219121}.