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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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