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cusB copper/silver export system membrane fusion protein [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945189, updated on 2-May-2024

Summary

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Gene symbol
cusB
Gene description
copper/silver export system membrane fusion protein
Primary source
ASAP:ABE-0001969
Locus tag
b0574
See related
ECOCYC:G6322
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
ECK0566; ylcD
Summary
cusB is in the cusCFBA Cu/Ag efflux operon regulated by Cu and Ag. [More information is available at EcoGene: EG14235]. CusB is a membrane fusion protein involved in the detoxification of copper and silver ions in Escherichia coli as part of the CusCFBA copper/silver efflux system. [More information is available at EcoCyc: G6322].
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Genomic context

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Sequence:
NC_000913.3 (597479..598702)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene copper/silver export system outer membrane channel Neighboring gene copper/silver export system periplasmic binding protein Neighboring gene copper/silver export system RND permease Neighboring gene phenylalanine:H(+) symporter PheP

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. EPR Spectroscopy Targets Structural Changes in the E. coli Membrane Fusion CusB upon Cu(I) Binding. Meir A, et al. Biophys J, 2017 Jun 20. PMID 28636907, Free PMC Article
  2. Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CusB. Xu Y, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009 Jul 1. PMID 19574656, Free PMC Article
  3. N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF. Mealman TD, et al. Biochemistry, 2012 Aug 28. PMID 22812620, Free PMC Article
  4. Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry. Mealman TD, et al. Biochemistry, 2011 Apr 5. PMID 21323389, Free PMC Article
  5. Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Bagai I, et al. Biochemistry, 2008 Nov 4. PMID 18847219, Free PMC Article

See all (40) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. findings reveal CusB is a dimer in solution and the orientation of one molecule with respect to the other molecule changes upon Cu(I) coordination, resulting in a more compact CusB structure; these structural and topological changes upon Cu(I) binding probably play a role of a switch for opening the channel and transferring metal ions from CusB to CusC and out of the cell
    Title: EPR Spectroscopy Targets Structural Changes in the E. coli Membrane Fusion CusB upon Cu(I) Binding.
  2. N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF.
    Title: N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF.
  3. Data reveal that N-terminal region of CusB interacts with metal-binding face of CusF; these proteins transiently interact in a metal-dependent fashion.
    Title: Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
  4. Alpha-helical domain of CusB is folded into a three-helix bundle that interacts with CusC. N- and C-termini of CusB form the first beta-strand domain that interact with CusA. CusB consists of multiple binding sites for Cu(+) and Ag(+) ions.
    Title: Crystal structure of the membrane fusion protein CusB from Escherichia coli.
Submit: New GeneRIF Correction

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 copper ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables copper ion transmembrane transporter activity IGI
Inferred from Genetic Interaction
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables transition metal ion binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables transition metal ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables transmembrane transporter activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within copper ion export IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in copper ion export NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in copper ion transmembrane transport NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in copper ion transport IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within detoxification of copper ion IGI
Inferred from Genetic Interaction
more info
 PubMed 
acts_upstream_of_or_within detoxification of copper ion IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within intracellular copper ion homeostasis IGI
Inferred from Genetic Interaction
more info
 PubMed 
acts_upstream_of_or_within intracellular copper ion homeostasis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within plasma membrane copper ion transport IGI
Inferred from Genetic Interaction
more info
 PubMed 
acts_upstream_of_or_within response to copper ion IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within response to copper ion IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within response to silver ion IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within response to silver ion IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in response to toxic substance IEA
Inferred from Electronic Annotation
more info
  
involved_in response to toxic substance NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in silver ion transmembrane transport NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cell envelope IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
is_active_in outer membrane-bounded periplasmic space IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
copper/silver export system membrane fusion protein

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
    597479..598702
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415106.1 copper/silver export system membrane fusion protein [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415106.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7EK49
    Conserved Domains (1) summary
    PRK09783
    Location:1 → 407
    PRK09783; copper/silver efflux system membrane fusion protein CusB; Provisional
Nucleotide Protein
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