P64612 · ZAPE_ECOLI

Function

function

Reduces the stability of FtsZ polymers in the presence of ATP. Required for cell division under low-oxygen conditions. Hydrolyzes ATP but not GTP.

Miscellaneous

ZapE abundance has to be tightly regulated to allow cell division. Loss or overexpression of ZapE alters Z-ring stability and leads to bacterial filamentation (PubMed:24595368).

Features

Showing features for binding site.

137550100150200250300350
TypeIDPosition(s)Description
Binding site78-85ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell division site
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionphospholipid binding
Biological Processcell division

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cell division protein ZapE
  • Alternative names
    • Z ring-associated protein ZapE

Gene names

    • Name
      zapE
    • Synonyms
      yhcM
    • Ordered locus names
      b3232, JW3201

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P64612
  • Secondary accessions
    • P46442
    • Q2M8Y1

Proteomes

Subcellular Location

Cytoplasm
Note: Localizes to the constricting Z-ring during late stages of the cell division process.

Keywords

Phenotypes & Variants

Disruption phenotype

Mutants have no growth defect in aerobic conditions. However, inactivation leads to a stress-dependent elongated phenotype (in anaerobiosis or at temperatures over 37 degrees Celsius).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis84Abolishes ATPase activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001694871-375Cell division protein ZapE

Proteomic databases

Interaction

Subunit

Interacts with FtsZ.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the AFG1 ATPase family. ZapE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    375
  • Mass (Da)
    43,064
  • Last updated
    2004-10-11 v1
  • Checksum
    24866D51E551452D
MQSVTPTSQYLKALNEGSHQPDDVQKEAVSRLEIIYQELINSTPPAPRTSGLMARVGKLWGKREDTKHTPVRGLYMWGGVGRGKTWLMDLFYQSLPGERKQRLHFHRFMLRVHEELTALQGQTDPLEIIADRFKAETDVLCFDEFFVSDITDAMLLGGLMKALFARGITLVATSNIPPDELYRNGLQRARFLPAIDAIKQHCDVMNVDAGVDYRLRTLTQAHLWLSPLHDETRAQMDKLWLALAGGKRENSPTLEINHRPLATMGVENQTLAVSFTTLCVDARSQHDYIALSRLFHTVMLFDVPVMTRLMESEARRFIALVDEFYERHVKLVVSAEVPLYEIYQGDRLKFEFQRCLSRLQEMQSEEYLKREHLAG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U18997
EMBL· GenBank· DDBJ
AAA58034.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC76264.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE77275.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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