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minC Z-ring positioning protein MinC [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945744, updated on 3-Dec-2024

Summary

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Official Symbol
minC
Official Full Name
Z-ring positioning protein MinC
Primary source
ECOCYC:EG10596
Locus tag
b1176
See related
ASAP:ABE-0003941
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
ECK1164; minB
Summary
MinCD oscillates (migrates) between coating one half of the cell's membrane (minE ring to pole) to coating the other half every 40 secs, and this may help to identify the cell center. [More information is available at EcoGene: EG10596]. MinC acts to ensure correct placement of the septum during cell division by suppressing formation of septa at aberrant loci within the cell. [More information is available at EcoCyc: EG10596].
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Genomic context

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Sequence:
NC_000913.3 (1225385..1226080, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene Z-ring positioning protein MinE Neighboring gene Z-ring positioning protein MinD Neighboring gene PF05666 family protein YcgJ Neighboring gene inhibitor of g-type lysozyme Neighboring gene protein YmgN

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. PSICIC: noise and asymmetry in bacterial division revealed by computational image analysis at sub-pixel resolution. Guberman JM, et al. PLoS Comput Biol, 2008 Nov. PMID 19043544, Free PMC Article
  2. "Division potential" in Escherichia coli. Donachie WD, et al. J Bacteriol, 1996 Oct. PMID 8830694, Free PMC Article
  3. Stability of the Escherichia coli division inhibitor protein MinC requires determinants in the carboxy-terminal region of the protein. Sen M, et al. J Bacteriol, 1998 Jan. PMID 9422610, Free PMC Article
  4. Targeted overexpression of the Escherichia coli MinC protein in higher plants results in abnormal chloroplasts. Tavva VS, et al. Plant Cell Rep, 2006 Apr. PMID 16341725
  5. The dimerization function of MinC resides in a structurally autonomous C-terminal domain. Szeto TH, et al. J Bacteriol, 2001 Nov. PMID 11673440, Free PMC Article

See all (120) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Min waves without MinC can pattern FtsA-anchored FtsZ filaments on model membranes.
    Title: Min waves without MinC can pattern FtsA-anchored FtsZ filaments on model membranes.
  2. The results suggest that DicB is a pleiotropic regulator of bacterial physiology and cell division and that these effects are mediated by a key molecular interaction with the cell division protein MinC.
    Title: Cryptic-Prophage-Encoded Small Protein DicB Protects Escherichia coli from Phage Infection by Inhibiting Inner Membrane Receptor Proteins.
  3. 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.
  4. Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division has been presented.
    Title: Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division.
  5. 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.
  6. 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.
  7. In the process of E. coli cell division, MinC-MinD copolymers bind to membrane, interact with FtsZ, and are disassembled by MinE.
    Title: MinCD cell division proteins form alternating copolymeric cytomotive filaments.
  8. The MinCDE proteins prevent the formation of the Z-ring at poles by oscillating from pole to pole, thereby ensuring that the concentration of the Z-ring inhibitor, MinC, is lowest at the cell center.
    Title: MinC, MinD, and MinE drive counter-oscillation of early-cell-division proteins prior to Escherichia coli septum formation.
  9. The binding sites for MinC and MinE overlap and reveals that they are at the MinD dimer interface.
    Title: Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.
  10. Taken together, these data indicate that polar Z rings are more susceptible to MinC/MinD than internal Z rings, even when MinE is absent.
    Title: Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli.
Submit: New GeneRIF Correction See all GeneRIFs (14)

Pathways from PubChem

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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 enzyme inhibitor activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables identical protein binding IDA
Inferred from Direct Assay
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 morphogenesis IEA
Inferred from Electronic Annotation
more info
  
involved_in cell septum assembly IEA
Inferred from Electronic Annotation
more info
  
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 division septum site selection IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of cell cycle IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of cell division IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of cell septum assembly IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cell pole IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
Z-ring positioning protein MinC

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
    1225385..1226080 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415694.1 Z-ring positioning protein MinC [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415694.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A7I6H3C0
    Conserved Domains (1) summary
    PRK03511
    Location:1 → 231
    minC; septum site-determining protein MinC
Nucleotide Protein
Heading Accession and Version

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