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rbn ribonuclease BN [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946760, updated on 26-Mar-2025
Official Symbol
rbn
Official Full Name
ribonuclease BN
Primary source
ECOCYC:G7175
Locus tag
b2268
See related
ASAP:ABE-0007496
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
ECK2262; ecoZ; elaC; rnz; zipD
Summary
RNase BN is required for MazF-mediated cell death after inhibition of translation (Amitai, 2009). yihY was previously thought to be rbn. [More information is available at EcoGene: EG14260]. RNase BN, also identified as binuclear zinc phosphodiesterase, cleaves the 3'-terminal portion of tRNAs as well as various short unstructured RNAs. [More information is available at EcoCyc: G7175].
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Sequence:
NC_000913.3 (2381608..2382525)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene tail-anchored inner membrane protein ElaB Neighboring gene putative acetyltransferase ElaA Neighboring gene protease ElaD Neighboring gene IPR002035/DUF3520 domain-containing protein YfbK

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. A mutant of escherichia coli defective in removing 3' terminal nucleotides from some transfer RNA precursor molecules. Seidman JG, et al. Cell, 1975 Aug. PMID 1098779
  2. Ribonuclease BN: identification and partial characterization of a new tRNA processing enzyme. Asha PK, et al. Proc Natl Acad Sci U S A, 1983 Jun. PMID 6344080, Free PMC Article
  3. ElaC encodes a novel binuclear zinc phosphodiesterase. Vogel A, et al. J Biol Chem, 2002 Aug 9. PMID 12029081
  4. Identification of metal binding residues for the binuclear zinc phosphodiesterase reveals identical coordination as glyoxalase II. Vogel A, et al. Biochemistry, 2004 Aug 17. PMID 15301536
  5. Characterization of an Escherichia coli elaC deletion mutant. Schilling O, et al. Biochem Biophys Res Commun, 2004 Aug 6. PMID 15303284

See all (34) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. These data indicate that RNase BN plays an important role in determining levels of the global transcription regulator, 6S RNA, throughout the growth cycle.
    Title: Growth Phase-dependent Variation of RNase BN/Z Affects Small RNAs: REGULATION OF 6S RNA.
  2. metal selectivity of ZiPD only partially relies on first shell metal ligands
    Title: Zinc- and iron-dependent cytosolic metallo-beta-lactamase domain proteins exhibit similar zinc-binding affinities, independent of an atypical glutamate at the metal-binding site.
  3. A ZiPD exosite is identified that guides physiological substrate recognition in the ZiPD/ElaC protein family.
    Title: Exosite modules guide substrate recognition in the ZiPD/ElaC protein family.
  4. the first crystal structure of ZiPD determined by multiple anomalous diffraction at a resolution of 2.9 A
    Title: The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins.
  5. the RNase Z homologue encoded by Escherichia coli elaC gene is RNase BN
    Title: The RNase Z homologue encoded by Escherichia coli elaC gene is RNase BN.
  6. These results suggest a potentially important new role for the RNase Z family of proteins in RNA metabolism, particularly in organisms lacking RNase E.
    Title: RNase Z in Escherichia coli plays a significant role in mRNA decay.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables 3'-tRNA processing endoribonuclease activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 3'-tRNA processing endoribonuclease activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables RNA endonuclease activity, producing 5'-phosphomonoesters IDA
Inferred from Direct Assay
more info
 PubMed 
enables RNA endonuclease activity, producing 5'-phosphomonoesters IEA
Inferred from Electronic Annotation
more info
  
enables RNA exonuclease activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables RNA exonuclease activity, producing 5'-phosphomonoesters IDA
Inferred from Direct Assay
more info
 PubMed 
enables endonuclease activity IEA
Inferred from Electronic Annotation
more info
  
enables exonuclease activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables nuclease activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables nuclease activity IEA
Inferred from Electronic Annotation
more info
  
enables protein homodimerization activity IPI
Inferred from Physical Interaction
more info
 PubMed 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in tRNA 3'-end processing IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within tRNA processing IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in tRNA processing IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
ribonuclease BN
NP_416771.4

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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
    2381608..2382525
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416771.4 ribonuclease BN [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416771.4

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7EAN6
    Conserved Domains (1) summary
    TIGR02649
    Location:3 → 305
    true_RNase_BN; ribonuclease BN
Nucleotide Protein
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