HAMAP rule MF_00720
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00720 |
| Accession | MF_00720 |
| Dates | 28-FEB-2005 (Created)
04-FEB-2025 (Last updated, Version 16) |
| Name | PriB |
| Scope(s) |
Bacteria Betaproteobacteria Gammaproteobacteria |
| Template(s) | P07013; Q5F924; A6THB2; [ Recover all ] |
| Triggered by |
HAMAP; MF_00720 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | PRIB |
| Protein name | RecName: Full=Replication restart protein PriB; |
| Gene name | Name=priB; |
Comments
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| FUNCTION | Involved in the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication; the PriA-PriB pathway is the major replication restart pathway. During primosome assembly it facilitates complex formation between PriA and DnaT on DNA; stabilizes PriA on DNA. Stimulates the DNA unwinding activity of PriA helicase. |
| SUBUNIT | Homodimer. Interacts with PriA and DnaT. Component of the replication restart primosome. Primosome assembly occurs via a 'hand- off' mechanism. PriA binds to replication forks, subsequently PriB then DnaT bind; DnaT then displaces ssDNA to generate the helicase loading substrate. |
| SIMILARITY | Belongs to the PriB family. |
Keywords
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Gene Ontology
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| GO:0003697; Molecular function:single-stranded DNA binding |
| GO:0006261; Biological process:DNA-templated DNA replication |
| GO:1990077; Cellular component:primosome complex |
Cross-references
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| Pfam | PF22657; SSB_1; 1; |
| PIRSF | PIRSF003135; Primosomal_n; 1; |
| NCBIfam | TIGR04418; PriB_gamma; 1; |
| PROSITE | PS50935; SSB; 1; |
Features
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Additional information
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| 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). |