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HAMAP rule MF_01485

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_01485
Accession MF_01485
Dates 10-DEC-2013 (Created)
02-SEP-2024 (Last updated, Version 22)
Name RecB
Scope(s) Bacteria
Actinomycetota
Bacteroidota
Chlamydiota
Chlorobiota
Deferribacteres
Pseudomonadota
Spirochaetota
Template(s) P08394; [ Recover all ]
Triggered by HAMAP; MF_01485 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier RECB
Protein name RecName: Full=RecBCD enzyme subunit RecB;
                 EC=3.1.11.5;
                 EC=5.6.2.4;
AltName: Full=DNA 3'-5' helicase subunit RecB;
AltName: Full=Exonuclease V subunit RecB;
                 Short=ExoV subunit RecB;
AltName: Full=Helicase/nuclease RecBCD subunit RecB;
Gene name Name=recB;

Comments [?]

FUNCTIONA helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA.
CATALYTIC ACTIVITY Reaction=Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- phosphooligonucleotides.; EC=3.1.11.5;
CATALYTIC ACTIVITY Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4;
CATALYTIC ACTIVITY Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
case <FTGroup:1>
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
end case
SUBUNITHeterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with RecA.
DOMAINThe N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC.
DOMAINThe C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA.
MISCELLANEOUSIn the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'- 3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site.
SIMILARITYBelongs to the helicase family. UvrD subfamily.

Keywords [?]


Gene Ontology [?]

case <FTGroup:1>
GO:0000287; Molecular function:magnesium ion binding
end case
GO:0043138; Molecular function:3'-5' DNA helicase activity
GO:0005524; Molecular function:ATP binding
GO:0003677; Molecular function:DNA binding
GO:0000724; Biological process:double-strand break repair via homologous recombination

Cross-references [?]

PROSITE PS51198; UVRD_HELICASE_ATP_BIND; 1;
PROSITE PS51217; UVRD_HELICASE_CTER; 1;
Pfam PF00580; UvrD-helicase; 1;
Pfam PF13361; UvrD_C; 1;
NCBIfam TIGR00609; recB; 1;

Features [?]

From: RECB_ECOLI (P08394)
Key From To Description Tag Condition FTGroup
REGION Nter 850 /note="DNA-binding and helicase activity, interacts with RecC"
REGION 900 Cter /note="Nuclease activity, interacts with RecD and RecA"
ACT_SITE 1080 1080 /note="For nuclease activity" D 1
BINDING 956 956 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
H 1
BINDING 1067 1067 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
D 1
BINDING 1080 1080 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
D 1

Additional information [?]

Size range 987-1496 amino acids
Related rules None
Fusion Nter: None Cter: None



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