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minD Z-ring positioning protein MinD [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945741, updated on 3-Dec-2024

Summary

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Official Symbol
minD
Official Full Name
Z-ring positioning protein MinD
Primary source
ECOCYC:EG10597
Locus tag
b1175
See related
ASAP:ABE-0003938
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
ECK1163; minB
Summary
The membrane localization of MinD is mediated by an 8-12 residue C-terminal motif, the membrane targeting sequence (MTS), mutations in this region prevent membrane localization, but not MinC binding. [More information is available at EcoGene: EG10597]. MinD recruits MinC to the membrane to form the MinC-MinD complex, which inhibits septum formation, and MinE acts to localize and restrict inhibition to the inappropriate septation sites . [More information is available at EcoCyc: EG10597].
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Genomic context

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Sequence:
NC_000913.3 (1224549..1225361, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene pseudo Neighboring gene Z-ring positioning protein MinE Neighboring gene Z-ring positioning protein MinC Neighboring gene PF05666 family protein YcgJ

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. The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: crystallization and preliminary X-ray analysis. Sakai N, et al. Acta Crystallogr D Biol Crystallogr, 2001 Jun. PMID 11375522
  2. Subcellular Min oscillations as a single-cell reporter of the action of polycations, protamine, and gentamicin on Escherichia coli. Downing BP, et al. PLoS One, 2009 Sep 30. PMID 19789705, Free PMC Article
  3. Modelling of processes governing subcellular localisation of MinD in Escherichia coli. Xu X, et al. IET Syst Biol, 2008 Sep. PMID 19045823
  4. Mutual effects of MinD-membrane interaction: I. Changes in the membrane properties induced by MinD binding. Mazor S, et al. Biochim Biophys Acta, 2008 Nov. PMID 18760994, Free PMC Article
  5. Mutual effects of MinD-membrane interaction: II. Domain structure of the membrane enhances MinD binding. Mazor S, et al. Biochim Biophys Acta, 2008 Nov. PMID 18760260, Free PMC Article

See all (176) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The bacterial division protein MinDE has an independent function in flagellation.
    Title: The bacterial division protein MinDE has an independent function in flagellation.
  2. Degradation of MinD oscillator complexes by Escherichia coli ClpXP.
    Title: Degradation of MinD oscillator complexes by Escherichia coli ClpXP.
  3. Non-Equilibrium Large-Scale Membrane Transformations Driven by MinDE Biochemical Reaction Cycles.
    Title: Non-Equilibrium Large-Scale Membrane Transformations Driven by MinDE Biochemical Reaction Cycles.
  4. The authors identified amino acids in both the N- and C-domains of MinC that are important for direct interactions with FtsZ and MinD in vitro, as well as mutations that modify the observed in vivo oscillation of green fluorescent protein (GFP)-MinC fusion protein.
    Title: MinC N- and C-Domain Interactions Modulate FtsZ Assembly, Division Site Selection, and MinD-Dependent Oscillation in Escherichia coli.
  5. The MinDE reaction-diffusion system can dictate the localization of membrane proteins in a spatiotemporal manner without specific molecular interactions in vitro. These proteins apparently establish a generic, nucleotide-dependent transport mode for membrane-bound diffusive molecules based on a moving diffusion barrier.
    Title: The MinDE system is a generic spatial cue for membrane protein distribution in vitro.
  6. This review summarizes the cell-free data supporting a molecular mechanism that explains the variety of patterns supported by MinD and MinE both in and out of the cell; with an emphasis on the recent appreciation for how multiple conformational states of MinE can drive oscillation by spatiotemporally regulating MinD interaction with the membrane.
    Title: Mechanistic insights of the Min oscillator via cell-free reconstitution and imaging.
  7. the dynamic association of the MTS with the beta-sheet is fine-tuned to balance MinE's need to sense MinD on the membrane with its need to diffuse in the cytoplasm, both of which are necessary for the oscillation
    Title: MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation.
  8. Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli.
    Title: Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli.
  9. membrane targeting sequence defines the lower limit of the concentration-dependent wavelength of Min protein patterns while restraining MinE's ability to stimulate MinD's ATPase activity.
    Title: Large-scale modulation of reconstituted Min protein patterns and gradients by defined mutations in MinE's membrane targeting sequence.
  10. a membrane anchored MinC/MinD complex is targeted to the Z ring through the conserved carboxy tail of FtsZ leading to breakage of FtsZ filaments.
    Title: MinC/MinD copolymers are not required for Min function.
Submit: New GeneRIF Correction See all GeneRIFs (33)

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP hydrolysis activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATP hydrolysis activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in cell division IEA
Inferred from Electronic Annotation
more info
  
involved_in cell division IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in chromosome segregation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in division septum assembly IEA
Inferred from Electronic Annotation
more info
  
involved_in division septum site selection IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in intracellular mRNA localization IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in cell pole IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in cytoplasmic side of plasma membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasmic side of plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane IMP
Inferred from Mutant Phenotype
more info
 PubMed 

General protein information

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Preferred Names
Z-ring positioning protein MinD

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
    1224549..1225361 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415693.1 Z-ring positioning protein MinD [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415693.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S0FV20
    Conserved Domains (1) summary
    PRK10818
    Location:1 → 270
    PRK10818; septum site-determining protein MinD
Nucleotide Protein
Heading Accession and Version

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