recD

UniProt ID: Q88DZ6
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
Aliases:
PP_4672
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Gene Description

RecD is the fast 5-prime-to-3-prime ATP-dependent DNA helicase motor of the bacterial RecBCD complex. Together with the oppositely directed RecB motor and the RecC scaffold, it drives processive double-strand-end unwinding and modulates RecB nuclease and RecA-loading activities. RecD contributes to, but does not itself catalyze, Exonuclease V nuclease chemistry. In the experimentally studied pseudomonad Pseudomonas syringae, RecD is required for resistance to UV and mitomycin C, unlike the dispensable RecD subunit in the corresponding Escherichia coli assays.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000724 double-strand break repair via homologous recombination
IEA
GO_REF:0000104
ACCEPT
Summary: The RecD motor is required for productive RecBCD-dependent homologous double-strand-break repair in pseudomonads.
Reason: The target record assigns RecD to recombinational end processing, and P. syringae recD mutants are UV- and mitomycin-C-sensitive; this contrasts with E. coli and supports retaining RecD as a core pseudomonad repair subunit.
Supporting Evidence:
PMID:20195537
sensitive to DNA-damaging agents and fail to grow at 4 degrees C.
file:PSEPK/recD/recD-uniprot.txt
facilitates RecA-binding to the ssDNA for homologous DNA recombination
GO:0003677 DNA binding
IEA
GO_REF:0000104
KEEP AS NON CORE
Summary: RecD contacts DNA in the RecBCD holoenzyme, although DNA binding alone does not define its motor role.
Reason: The target record explicitly says that every RecBCD subunit contributes to DNA binding; the directional helicase term remains the informative core molecular function.
Supporting Evidence:
file:PSEPK/recD/recD-uniprot.txt
All subunits contribute to DNA-binding.
GO:0004386 helicase activity
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: RecD genuinely has helicase activity, but this generic term is less informative than its directional motor assignment.
Reason: Retain the true broad molecular function while using GO:0043139, 5-prime-to-3-prime DNA helicase activity, as the defining core term.
Supporting Evidence:
file:PSEPK/recD/recD-uniprot.txt
ssDNA-dependent ATPase and 5'-3' helicase activity.
GO:0005524 ATP binding
IEA
GO_REF:0000104
ACCEPT
Summary: ATP binding is intrinsic to the RecD ATPase-helicase motor.
Reason: The target record assigns RecD an ATP-hydrolysis reaction and ATP-dependent 5-prime-to-3-prime helicase activity.
Supporting Evidence:
file:PSEPK/recD/recD-uniprot.txt
Reaction=ATP + H2O = ADP + phosphate + H(+)
GO:0006302 double-strand break repair
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: RecD participates in double-strand-break repair, but GO:0000724 captures the homologous-recombination route more precisely.
Reason: P. syringae recD mutants are sensitive to UV and mitomycin C and lose RecBCD recombination proficiency, providing direct pseudomonad support for the broad process while the more specific homologous-repair term remains core.
Supporting Evidence:
PMID:20195537
sensitive to DNA-damaging agents and fail to grow at 4 degrees C.
GO:0006310 DNA recombination
IEA
GO_REF:0000120
ACCEPT
Summary: RecD powers the RecBCD end-processing pathway that initiates homologous DNA recombination.
Reason: The target record links RecD-containing holoenzyme activity to RecA loading, and pseudomonad RecBCD clones confer recombination proficiency.
Supporting Evidence:
PMID:2559208
Three clones from Pseudomonas aeruginosa and Ps. putida conferred recombination proficiency and ATP-dependent nuclease activity
file:PSEPK/recD/recD-uniprot.txt
facilitates RecA-binding to the ssDNA for homologous DNA recombination
GO:0008854 exodeoxyribonuclease V activity
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: RecD stimulates and contributes to Exonuclease V activity but does not independently catalyze nuclease chemistry.
Reason: The `enables` qualifier incorrectly attributes the holoenzyme's nuclease reaction directly to RecD. The target record states that RecD stimulates RecBC nuclease activity; the catalytic nuclease site is in RecB.
Supporting Evidence:
file:PSEPK/recD/recD-uniprot.txt
assembled RecBC greatly stimulates nuclease activity and augments
GO:0009338 exodeoxyribonuclease V complex
IEA
GO_REF:0000120
ACCEPT
Summary: RecD is the 5-prime-to-3-prime motor subunit of the Exonuclease V complex.
Reason: The target record explicitly identifies the RecB-RecC-RecD heterotrimer, and pseudomonad genetic evidence shows that RecD loss functionally disables RecBCD.
Supporting Evidence:
file:PSEPK/recD/recD-uniprot.txt
Heterotrimer of RecB, RecC and RecD.
PMID:20195537
The RecD requirement is only a function of the RecBCD complex
GO:0016887 ATP hydrolysis activity
IEA
GO_REF:0000120
ACCEPT
Summary: RecD hydrolyzes ATP to power its directional DNA motor.
Reason: The target record supplies the explicit Rhea ATP-hydrolysis reaction and identifies RecD as an ssDNA-dependent ATPase.
Supporting Evidence:
file:PSEPK/recD/recD-uniprot.txt
Reaction=ATP + H2O = ADP + phosphate + H(+)
GO:0017116 single-stranded DNA helicase activity
IEA
GO_REF:0000118
KEEP AS NON CORE
Summary: RecD has directly supported single-stranded-DNA-dependent helicase activity, a substrate-axis description distinct from motor directionality.
Reason: GO:0017116 is not a parent of the 5-prime-to-3-prime term and is biologically true, but GO:0043139 better captures RecD's defining polarity in the core-function summary.
Supporting Evidence:
file:PSEPK/recD/recD-uniprot.txt
ssDNA-dependent ATPase and 5'-3' helicase activity.
GO:0043139 5'-3' DNA helicase activity
IEA
GO_REF:0000120
ACCEPT
Summary: RecD is the fast 5-prime-to-3-prime DNA helicase motor of RecBCD.
Reason: The target record explicitly assigns 5-prime-to-3-prime helicase activity to this RecD family protein and describes ATP-coupled translocation in that direction.
Supporting Evidence:
file:PSEPK/recD/recD-uniprot.txt
ssDNA-dependent ATPase and 5'-3' helicase activity.

Core Functions

Provides the fast 5-prime-to-3-prime ATP-dependent helicase motor that drives RecBCD end unwinding and modulates holoenzyme processivity.

Supporting Evidence:
  • file:PSEPK/recD/recD-uniprot.txt
    ssDNA-dependent ATPase and 5'-3' helicase activity.
  • PMID:20195537
    The RecD requirement is only a function of the RecBCD complex

References

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Suggested Questions for Experts

Q: How do RecD motor speed and ATPase activity tune RecA loading and the resection-mode switch in the KT2440 RecBCD complex?

Suggested Experiments

Experiment: Test a clean recD deletion for double-strand-break repair, homologous recombination, and RecA loading, then complement with wild-type protein.

Type: genetic pathway validation

πŸ“š Additional Documentation

Notes

(recD-notes.md)

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