sopB

UniProt ID: P62558
Organism: Escherichia coli K-12
Review Status: DRAFT
Aliases:
ECOK12F047
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Gene Description

SopB is the centromere-binding protein of the F plasmid partition system. It binds the sopC centromere, a cluster of 43-bp repeats, through an all-helical DNA-binding domain attached to a dimerization domain, and coats flanking DNA to form the partition complex. SopB is a CTPase whose activity is stimulated by sopC DNA, and CTP promotes loading of multiple SopB molecules onto sopC-containing DNA. Bound at sopC, SopB recruits the partition ATPase SopA and stimulates its ATP hydrolysis by contributing an arginine finger, which drives positioning and separation of plasmid copies. SopB also acts with SopA to repress the sopAB operon and silences genes near sopC.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003677 DNA binding
IEA
GO_REF:0000002
MODIFY
Summary: SopB binds DNA; its defining activity is sequence-specific binding to the sopC centromere.
Reason: True but less specific than the evidence. Purified SopB binds the sopC repeats specifically, and crystal structures show SopB bound to its site. It also coats non-specific DNA, but recognition of sopC is the activity that defines it. Sequence-specific DNA binding (GO:0043565) is a descendant of DNA binding and is the term used for chromosomal ParB.
Proposed replacements: sequence-specific DNA binding
Supporting Evidence:
PMID:2670941
SopB protein binds to the sopC region, in which 12 direct repeats of 43-base pairs nucleotides exist.
PMID:20236989
it binds sopC to form a partition complex, which recruits SopA
GO:0043565 sequence-specific DNA binding
IDA
PMID:2670941
Purification and characterization of SopA and SopB proteins ...
NEW
Summary: SopB binds the sopC centromere repeats.
Reason: The replacement for the electronic DNA binding row, recorded with its experimental source (gel retardation and footprinting of purified SopB, and SopB-DNA crystal structures).
Supporting Evidence:
PMID:2670941
SopB protein binds to the sopC region, in which 12 direct repeats of 43-base pairs nucleotides exist.
PMID:20236989
it binds sopC to form a partition complex, which recruits SopA
GO:0043273 CTPase activity
IDA
PMID:34286695
CTP and parS coordinate ParB partition complex dynamics and ...
NEW
Summary: Purified SopB (ParB of F) hydrolyses CTP, stimulated by sopC DNA.
Reason: Direct measurement on the F plasmid protein, called ParBF in the paper (the F system is SopA/B/C). Hydrolysis is specific for CTP and follows Michaelis-Menten kinetics, with the maximum rate raised about threefold by sopC DNA. CTP promotes loading of multiple SopB molecules onto sopC-containing DNA, the clamp behaviour shared with chromosomal ParB.
Supporting Evidence:
PMID:34286695
using F-plasmid ParAFBFSF (also called SopA/B/C) as a model system
PMID:34286695
ParBF had negligible activity for all NTPs other than CTP
GO:0001671 ATPase activator activity
IDA
PMID:19740757
Dual role of DNA in regulating ATP hydrolysis by the SopA pa...
NEW
Summary: SopB stimulates SopA ATP hydrolysis through an arginine finger.
Reason: SopB does not bind ATP itself but stimulates the ATPase of its partner: purified SopB raises SopA ATP hydrolysis above the DNA-stimulated level, and it provides the catalytic arginine finger. This is the coupling between the two partition roles, and the activity that drives separation of the partition complexes.
Supporting Evidence:
PMID:1406581
The ATPase activity in the presence of DNA was further stimulated by addition of the SopB protein.
PMID:19740757
which we show here to provide an arginine-finger motif
GO:0030541 plasmid partitioning
IMP
PMID:10395819
The F plasmid centromere, sopC, is required for full repress...
NEW
Summary: SopB is required for F plasmid partition.
Reason: SopB does work in the process: it forms the partition complex at sopC and activates SopA. sopB missense mutants were isolated by screening for unstable inheritance of mini-F.
Supporting Evidence:
PMID:10395819
We have isolated sop mutants by screening for unstable inheritance of mutagenized mini-F DNA.
PMID:10395819
Four of the mutants resulted from different missense mutations in sopB.
GO:0045892 negative regulation of DNA-templated transcription
IMP
PMID:9529520
Autoregulation of the partition genes of the mini-F plasmid ...
NEW
Summary: SopB, with SopA, represses the sopAB operon.
Reason: Repression needs SopA and SopB together; SopB alone does not bind the operator but enhances SopA binding there, and sopC strengthens the repression. Non-core: it keeps Sop protein levels in the range that partition needs.
Supporting Evidence:
PMID:9529520
the sopAB operon is repressed by the cooperative action of SopA and SopB
PMID:10395819
it interacts with SopA to repress transcription of the sopAB operon
GO:0002135 CTP binding
IC
PMID:34286695
CTP and parS coordinate ParB partition complex dynamics and ...
NEW
Summary: SopB binds the CTP it hydrolyses, and CTP promotes its loading on sopC.
Reason: Curator inference from the measured, CTP-specific hydrolysis by purified SopB (ParBF), which requires CTP binding. Recorded separately because GO does not derive CTP binding from CTPase activity.
Supporting Evidence:
PMID:34286695
ParBF had negligible activity for all NTPs other than CTP

Core Functions

Binds the sopC centromere and, as a CTP-dependent clamp, forms the partition complex on F plasmid DNA.

Directly Involved In:
Supporting Evidence:
  • PMID:2670941
    SopB protein binds to the sopC region, in which 12 direct repeats of 43-base pairs nucleotides exist.

sopC-stimulated CTP hydrolysis that controls SopB loading onto sopC DNA.

Molecular Function:
CTPase activity
Directly Involved In:
Supporting Evidence:

Stimulates ATP hydrolysis by nucleoid-bound SopA through an arginine finger, driving separation of the partition complexes.

Molecular Function:
ATPase activator activity
Directly Involved In:
Supporting Evidence:

References

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Suggested Questions for Experts

Q: Are the CTP-bound clamp state and the arginine-finger stimulation of SopA linked, so that SopB activates SopA only when loaded on sopC?

Suggested Experiments

Experiment: Measure SopA ATPase stimulation by SopB in CTP, CTPgammaS and no-nucleotide conditions, with and without sopC DNA.

Hypothesis: CTP-dependent clamping of SopB on sopC is required for efficient activation of SopA.

Type: enzyme assay

πŸ“š Additional Documentation

Notes

(sopB-notes.md)

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