UniProt functional annotation for P23478



	UniProt functional annotation for P23478

UniProt code: P23478.

Organism: Bacillus subtilis (strain 168).

Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.

Function: An essential component of the DNA double-stranded break repair machinery, the heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' -> 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddA nuclease domain in particular is required for chi fragment generation; this subunit has 3' -> 5' nuclease and helicase activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB. {ECO:0000269|PubMed:10756102, ECO:0000269|PubMed:17570399, ECO:0000269|PubMed:8387145}.

Catalytic activity: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10756102}; Note=At low magnesium concentrations there is no nuclease activity, but helicase activity is unaffected. {ECO:0000269|PubMed:10756102};

Subunit: Heterodimer of AddA and AddB. {ECO:0000269|PubMed:19129187, ECO:0000269|PubMed:8387145}.

Miscellaneous: This enzyme is a functional homolog of the E.coli RecBCD enzyme; unlike the RecBCD enzyme it degrades both duplex strands symmetrically.

Similarity: Belongs to the helicase family. AddA subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bacillus subtilis (strain 168).
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.



Function:		An essential component of the DNA double-stranded break repair machinery, the heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' -> 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddA nuclease domain in particular is required for chi fragment generation; this subunit has 3' -> 5' nuclease and helicase activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB. {ECO:0000269\|PubMed:10756102, ECO:0000269\|PubMed:17570399, ECO:0000269\|PubMed:8387145}.


Catalytic activity:		Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:10756102}; Note=At low magnesium concentrations there is no nuclease activity, but helicase activity is unaffected. {ECO:0000269\|PubMed:10756102};
Subunit:		Heterodimer of AddA and AddB. {ECO:0000269\|PubMed:19129187, ECO:0000269\|PubMed:8387145}.
Miscellaneous:		This enzyme is a functional homolog of the E.coli RecBCD enzyme; unlike the RecBCD enzyme it degrades both duplex strands symmetrically.
Similarity:		Belongs to the helicase family. AddA subfamily. {ECO:0000305}.