AC   MF_00720;
DC   Protein; auto
TR   HAMAP; MF_00720; -; 1; level=0
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Names: PriB
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ID   PRIB
DE   RecName: Full=Primosomal replication protein N;
GN   Name=priB;
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case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
CC   -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site
CC       (PAS). During primosome assembly it facilitates the complex formation
CC       between PriA and DnaT.
CC   -!- SUBUNIT: Component of the preprimosomal complex composed of one monomer
CC       of PriC and DnaT, two monomers of PriA, two dimers of PriB and one
CC       hexamer of DnaB. Upon transient interaction with DnaG it forms the
CC       primosome.
else case <OC:Neisseria>
CC   -!- FUNCTION: Stimulates the DNA unwinding activity of PriA helicase, which
CC       does not seem to require single-stranded DNA-binding by PriB. Activates
CC       DNA-dependent ATP hydrolysis catalyzed by PriA.
CC   -!- SUBUNIT: Homodimer. Component of the preprimosomal complex.
else
CC   -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site
CC       (PAS).
CC   -!- SUBUNIT: Component of the preprimosomal complex composed of PriA, PriB,
CC       PriC, DnaB and DnaT. Upon transient interaction with DnaG it forms the
CC       primosome.
end case
CC   -!- SIMILARITY: Belongs to the PriB family.
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DR   Pfam; PF00436; SSB; 1; trigger=no
DR   PIRSF; PIRSF003135; Primosomal_n; 1; trigger=no
DR   NCBIfam; TIGR04418; PriB_gamma; 1; trigger=no
DR   PROSITE; PS50935; SSB; 1; trigger=yes
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KW   DNA replication
KW   Primosome
KW   DNA-binding
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GO   GO:0003697; F:single-stranded DNA binding
GO   GO:0006260; P:DNA replication
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FT   None
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Size: 90-130;
Related: None;
Template: P07013; Q5F924;
Scope:
 Bacteria; Betaproteobacteria
 Bacteria; Gammaproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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).
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# Revision 1.17 2023/06/01
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