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.
| 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 |
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Download this section (compressed HTML)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?
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
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