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    priB primosomal replication protein N [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948722, updated on 3-Dec-2024

    Summary

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    Official Symbol
    priB
    Official Full Name
    primosomal replication protein N
    Primary source
    ECOCYC:EG10764
    Locus tag
    b4201
    See related
    ASAP:ABE-0013742
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK4197
    Summary
    PriB is structural similar to Ssb. [More information is available at EcoGene: EG10764]. PriB is a component of the primosome, a multiprotein complex that is believed to be involved in restart of stalled replication forks. [More information is available at EcoCyc: EG10764].
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    Genomic context

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    Sequence:
    NC_000913.3 (4425520..4425834)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF1471 domain-containing protein YjfY Neighboring gene 30S ribosomal subunit protein S6 Neighboring gene 30S ribosomal subunit protein S18 Neighboring gene 50S ribosomal subunit protein L9

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Protein n, a primosomal DNA replication protein of Escherichia coli. Purification and characterization. Low RL, et al. J Biol Chem, 1982 Jun 10. PMID 6281262
    2. Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site. Shioi S, et al. Biochem Biophys Res Commun, 2005 Jan 28. PMID 15607735
    3. Crystal structure of PriB, a primosomal DNA replication protein of Escherichia coli. Liu JH, et al. J Biol Chem, 2004 Nov 26. PMID 15383524
    4. Isolation and characterization of a priB mutant of Escherichia coli influencing plasmid copy number of delta rop ColE1-type plasmids. Bergès H, et al. J Bacteriol, 1997 Feb. PMID 9006055, Free PMC Article
    5. Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode. Huang CY, et al. Nucleic Acids Res, 2006. PMID 16899446, Free PMC Article

    See all (41) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Identification of genetic interactions with priB links the PriA/PriB DNA replication restart pathway to double-strand DNA break repair in Escherichia coli.
      Title: Identification of genetic interactions with priB links the PriA/PriB DNA replication restart pathway to double-strand DNA break repair in Escherichia coli.
    2. A structural model of the PriB-DnaT complex in Escherichia coli replication restart.
      Title: A structural model of the PriB-DnaT complex in Escherichia coli replication restart.
    3. Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.
      Title: Structural insight into the DNA-binding mode of the primosomal proteins PriA, PriB, and DnaT.
    4. found that the acidic linker between the two domains had an activity for dissociating ssDNA from the PriB.ssDNA complexes in a manner supported by the conserved acidic residues Asp70 and Glu76
      Title: Structure and mechanism of the primosome protein DnaT-functional structures for homotrimerization, dissociation of ssDNA from the PriB·ssDNA complex, and formation of the DnaT·ssDNA complex.
    5. A role for His64 in the compactness of the PriB-ssDNA complex and in the positive cooperativity of PriB.
      Title: Involvement of histidine in complex formation of PriB and single-stranded DNA.
    6. Abolishing PriB leads to suppression of the recG null phenotype.
      Title: Modulation of DNA damage tolerance in Escherichia coli recG and ruv strains by mutations affecting PriB, the ribosome and RNA polymerase.
    7. Binding mode is proposed for forming a stable complex of PriB with ssDNA of 25 nucleotides.
      Title: A single residue determines the cooperative binding property of a primosomal DNA replication protein, PriB, to single-stranded DNA.
    8. PriB homolog of K. pneumoniae is similar in structure and in function to that of E. coli
      Title: The priB gene of Klebsiella pneumoniae encodes a 104-amino acid protein that is similar in structure and function to Escherichia coli PriB.
    9. Binding of the PriB dimer to the PriA- primosome assembly site complex dramatically increases PriA's affinity for the strong site, but only slightly affects its affinity for the weak site.
      Title: Binding of two PriA-PriB complexes to the primosome assembly site initiates primosome formation.
    10. N-terminus verified by Edman degradation on mature peptide
      Title: The priB and priC replication proteins of Escherichia coli. Genes, DNA sequence, overexpression, and purification.
    Submit: New GeneRIF Correction See all GeneRIFs (15)

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables DNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables single-stranded DNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables single-stranded DNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in DNA replication IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within DNA replication initiation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in DNA replication, synthesis of primer IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in DNA replication, synthesis of primer NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in DNA unwinding involved in DNA replication NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within plasmid maintenance IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in replication fork processing NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within response to radiation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of DnaB-DnaC-DnaT-PriA-PriB complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    part_of pre-primosome complex IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    part_of primosome complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of primosome complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    part_of replisome IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    primosomal replication protein N

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      4425520..4425834
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418622.1 primosomal replication protein N [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418622.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5C9A7U1
      Conserved Domains (1) summary
      PRK02801
      Location:1 → 101
      PRK02801; primosomal replication protein N; Provisional
    Nucleotide Protein
    Heading Accession and Version

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