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    zapA cell division protein ZapA [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947404, updated on 17-Dec-2024

    Summary

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    Official Symbol
    zapA
    Official Full Name
    cell division protein ZapA
    Primary source
    ECOCYC:EG12878
    Locus tag
    b2910
    See related
    ASAP:ABE-0009554
    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
    ECK2905; ygfE
    Summary
    ZapA binding promotes FtsZ polymer bundling and inhibits the GTPase activity of FtsZ (Small, 2007). [More information is available at EcoGene: EG12878]. ZapA binds to FtsZ polymers and promotes their bundling; it is a potent inhibitor of the GTPase activity of FtsZ . [More information is available at EcoCyc: EG12878].
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    Genomic context

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    Sequence:
    NC_000913.3 (3055612..3055941)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene 2-octaprenyl-6-methoxyphenol 4-hydroxylase Neighboring gene Xaa-Pro aminopeptidase Neighboring gene PF03695 family protein YgfB Neighboring gene ncRNA Neighboring gene putative 5-formyltetrahydrofolate cyclo-ligase

    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. Bacterial division: the fellowship of the ring. Margolin W. Curr Biol, 2003 Jan 8. PMID 12526758
    2. Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA. Caldas P, et al. Nat Commun, 2019 Dec 17. PMID 31848350, Free PMC Article
    3. Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli. Addinall SG, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005 Mar 1. PMID 16511026, Free PMC Article
    4. FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP. Small E, et al. J Mol Biol, 2007 May 25. PMID 17428494
    5. Investigating the effect of bacteriophages on bacterial FtsZ localisation. Dhanoa GK, et al. Front Cell Infect Microbiol, 2022. PMID 35967845, Free PMC Article

    See all (34) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Investigating the effect of bacteriophages on bacterial FtsZ localisation.
      Title: Investigating the effect of bacteriophages on bacterial FtsZ localisation.
    2. Study found that ZapA cooperatively increases the spatial order of the filament network but binds only transiently to FtsZ filaments and has no effect on filament length and treadmilling velocity. Together, data provides a model for how FtsZ-associated proteins can increase the precision and stability of the bacterial cell division machinery in a switch-like manner.
      Title: Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA.
    3. Data indicate a model of the cell division proteins FtsZ protofilamentZapA tetramer complex by information-driven docking with the HADDOCK2.2 webserver.
      Title: Mapping the Contact Sites of the Escherichia coli Division-Initiating Proteins FtsZ and ZapA by BAMG Cross-Linking and Site-Directed Mutagenesis.
    4. Data show that the replication terminus attaches to the divisome in a single segment along the perimeter of the cell in a MatP, ZapA and ZapB proteins-dependent manner.
      Title: The role of MatP, ZapA and ZapB in chromosomal organization and dynamics in Escherichia coli.
    5. These results suggest that the main function of ZapA and ZapB in vivo may not be to promote the association of individual protofilaments but to align FtsZ clusters that consist of multiple FtsZ protofilaments.
      Title: In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy.
    6. We generated a number of mutant forms of ZapA with the aim of disrupting the dimer-dimer interface. We show that one of these mutants, I83E, is fully folded and binds to FtsZ, but is a constitutive dimer.
      Title: Tetramerization of ZapA is required for FtsZ bundling.
    7. The authors propose a molecular model in which ZapA increases lateral interactions between FtsZ proto-filaments and ZapB mediates further stabilization of this interaction by cross-linking ZapA molecules bound to adjacent FtsZ proto-filaments.
      Title: Spatial resolution of two bacterial cell division proteins: ZapA recruits ZapB to the inner face of the Z-ring.
    8. The putative Escherichia coli ZapA orthologue, YgfE, exists in a dimer/tetramer equilibrium in solution, binds to FtsZ polymers, strongly promotes FtsZ polymer bundling and is a potent inhibitor of the FtsZ GTPase activity.
      Title: FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP.
    Submit: New GeneRIF Correction

    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 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 FtsZ-dependent cytokinesis IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in FtsZ-dependent cytokinesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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 cell division IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    involved_in cell septum assembly IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in division septum assembly IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in division septum assembly IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within division septum assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in septin ring assembly IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within septin ring assembly IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cell division site IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cell division site IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cell septum IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cell septum IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    cell division protein ZapA

    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
      3055612..3055941
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417386.1 cell division protein ZapA [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417386.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7EGA5
      Conserved Domains (1) summary
      PRK10972
      Location:1 → 109
      PRK10972; cell division protein ZapA
    Nucleotide Protein
    Heading Accession and Version

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