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Annotation rule MF_00720
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General rule information [?]

Accession MF_00720
Dates 24-OCT-2003 (Created)
18-NOV-2019 (Last updated, Version 16)
Name PriB
Scope
Bacteria; Betaproteobacteria
Bacteria; Gammaproteobacteria
Templates P07013 (PRIB_ECOLI); Q5F924 (PRIB_NEIG1): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
PRIB
Protein name
RecName: Full=Primosomal replication protein N;
Gene name
priB

Comments [?]

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
Function Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT.
Subunit Component of the preprimosomal complex composed of one monomer of PriC and DnaT, two monomers of PriA, two dimers of PriB and one hexamer of DnaB. Upon transient interaction with DnaG it forms the primosome.
else case <OC:Neisseria>
Function Stimulates the DNA unwinding activity of PriA helicase, which does not seem to require single-stranded DNA-binding by PriB. Activates DNA-dependent ATP hydrolysis catalyzed by PriA.
Subunit Homodimer. Component of the preprimosomal complex.
else
Function Binds single-stranded DNA at the primosome assembly site (PAS).
Subunit Component of the preprimosomal complex composed of PriA, PriB, PriC, DnaB and DnaT. Upon transient interaction with DnaG it forms the primosome.
end case
Similarity Belongs to the PriB family.

Keywords [?]


Gene Ontology [?]

GO:0003697; Molecular function: single-stranded DNA binding.
GO:0006260; Biological process: DNA replication.

Cross-references [?]

Pfam PF00436; SSB; 1;
PIRSF PIRSF003135; Primosomal_n; 1;
TIGRFAMs TIGR04418; PriB_gamma; 1;
PROSITE PS50935; SSB; 1; trigger=PRU00252;

Additional information [?]

Size range 90-130 amino acids
Related rules None
Fusion None
Comments For a reference on the evolution of this family, see: MEDLINE=22749900; PubMed=12867746; Ponomarev V.A., Makarova K.S., Aravind L., Koonin E.V.; "Gene duplication with displacement and rearrangement: origin of the bacterial replication protein PriB from the single-stranded DNA-binding protein Ssb."; J. Mol. Microbiol. Biotechnol. 5:225-229(2003).