P64612 · ZAPE_ECOLI
- ProteinCell division protein ZapE
- GenezapE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids375 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell division site | |
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | phospholipid binding | |
Biological Process | cell division |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCell division protein ZapE
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP64612
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the constricting Z-ring during late stages of the cell division process.
Keywords
- Cellular component
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 84 | Abolishes ATPase activity. | ||||
Sequence: K → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000169487 | 1-375 | Cell division protein ZapE | |||
Sequence: MQSVTPTSQYLKALNEGSHQPDDVQKEAVSRLEIIYQELINSTPPAPRTSGLMARVGKLWGKREDTKHTPVRGLYMWGGVGRGKTWLMDLFYQSLPGERKQRLHFHRFMLRVHEELTALQGQTDPLEIIADRFKAETDVLCFDEFFVSDITDAMLLGGLMKALFARGITLVATSNIPPDELYRNGLQRARFLPAIDAIKQHCDVMNVDAGVDYRLRTLTQAHLWLSPLHDETRAQMDKLWLALAGGKRENSPTLEINHRPLATMGVENQTLAVSFTTLCVDARSQHDYIALSRLFHTVMLFDVPVMTRLMESEARRFIALVDEFYERHVKLVVSAEVPLYEIYQGDRLKFEFQRCLSRLQEMQSEEYLKREHLAG |
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)43,064
- Last updated2004-10-11 v1
- Checksum24866D51E551452D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |