HAMAP rule MF_00720
General rule information
[?]
PURL | https://purl.expasy.org/hamap/rule/MF_00720 |
Accession | MF_00720 |
Dates | 24-OCT-2003 (Created)
1-JUN-2023 (Last updated, Version 17) |
Name | PriB |
Scope(s) |
Bacteria Betaproteobacteria Gammaproteobacteria |
Template(s) | P07013 (PRIB_ECOLI); Q5F924 (PRIB_NEIG1); [ Recover all ] |
Triggered by |
HAMAP; MF_00720 (Get profile general information and statistics) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Identifier | PRIB |
Protein name | RecName: Full=Primosomal replication protein N; |
Gene name | 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; |
NCBIfam | TIGR04418; PriB_gamma; 1; |
PROSITE | PS50935; SSB; 1; |
Features
[?]
Additional information
[?]
Size range | 90-130 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: 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). |