UniProt functional annotation for P77173



	UniProt functional annotation for P77173

UniProt code: P77173.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring (PubMed:9008158, PubMed:11847116, PubMed:22164258, PubMed:22304478, PubMed:23233671). Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL and FtsN (PubMed:11847116, PubMed:11948172). ZipA overproduction protects FtsZ from degradation by ClpP by preventing recognition by ClpX (PubMed:23233671). Does not affect the GTPase activity of FtsZ (PubMed:10209756). {ECO:0000269|PubMed:10209756, ECO:0000269|PubMed:11847116, ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:22164258, ECO:0000269|PubMed:22304478, ECO:0000269|PubMed:23233671, ECO:0000269|PubMed:9008158}.

Subunit: Interacts with FtsZ via their C-terminal domains (PubMed:9008158, PubMed:10209756, PubMed:10880432, PubMed:22164258). Can form homodimers prior to association with FtsZ (PubMed:22304478). {ECO:0000269|PubMed:10209756, ECO:0000269|PubMed:10880432, ECO:0000269|PubMed:22164258, ECO:0000269|PubMed:22304478, ECO:0000269|PubMed:9008158}.

Subcellular location: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:9008158}; Single-pass type I membrane protein {ECO:0000269|PubMed:9008158}. Note=Localizes to the Z ring in an FtsZ- dependent manner (PubMed:9008158, PubMed:9864327, PubMed:10209756). Localization does not depend upon FtsA or FtsI (PubMed:9864327, PubMed:10209756). {ECO:0000269|PubMed:10209756, ECO:0000269|PubMed:9008158, ECO:0000269|PubMed:9864327}.

Induction: Repressed 1.5-fold by hydroxyurea. {ECO:0000269|PubMed:20005847}.

Domain: Contains an N-terminal transmembrane domain, followed by a charged domain, an unstructured P/Q domain rich in proline and glutamine, and a C-terminal FtsZ-binding domain. {ECO:0000305|PubMed:12107152}.

Miscellaneous: Has been isolated as a 91 kDa complex containing ZipA- EptA and an unidentified 24 kDa protein (PubMed:16079137), but it was shown later that there is no physical interaction between ZipA and EptA (PubMed:22304478). {ECO:0000305|PubMed:16079137, ECO:0000305|PubMed:22304478}.

Similarity: Belongs to the ZipA family. {ECO:0000255|HAMAP- Rule:MF_00509, ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring (PubMed:9008158, PubMed:11847116, PubMed:22164258, PubMed:22304478, PubMed:23233671). Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL and FtsN (PubMed:11847116, PubMed:11948172). ZipA overproduction protects FtsZ from degradation by ClpP by preventing recognition by ClpX (PubMed:23233671). Does not affect the GTPase activity of FtsZ (PubMed:10209756). {ECO:0000269\|PubMed:10209756, ECO:0000269\|PubMed:11847116, ECO:0000269\|PubMed:11948172, ECO:0000269\|PubMed:22164258, ECO:0000269\|PubMed:22304478, ECO:0000269\|PubMed:23233671, ECO:0000269\|PubMed:9008158}.


Subunit:		Interacts with FtsZ via their C-terminal domains (PubMed:9008158, PubMed:10209756, PubMed:10880432, PubMed:22164258). Can form homodimers prior to association with FtsZ (PubMed:22304478). {ECO:0000269\|PubMed:10209756, ECO:0000269\|PubMed:10880432, ECO:0000269\|PubMed:22164258, ECO:0000269\|PubMed:22304478, ECO:0000269\|PubMed:9008158}.
Subcellular location:		Cell inner membrane {ECO:0000269\|PubMed:16079137, ECO:0000269\|PubMed:9008158}; Single-pass type I membrane protein {ECO:0000269\|PubMed:9008158}. Note=Localizes to the Z ring in an FtsZ- dependent manner (PubMed:9008158, PubMed:9864327, PubMed:10209756). Localization does not depend upon FtsA or FtsI (PubMed:9864327, PubMed:10209756). {ECO:0000269\|PubMed:10209756, ECO:0000269\|PubMed:9008158, ECO:0000269\|PubMed:9864327}.
Induction:		Repressed 1.5-fold by hydroxyurea. {ECO:0000269\|PubMed:20005847}.
Domain:		Contains an N-terminal transmembrane domain, followed by a charged domain, an unstructured P/Q domain rich in proline and glutamine, and a C-terminal FtsZ-binding domain. {ECO:0000305\|PubMed:12107152}.
Miscellaneous:		Has been isolated as a 91 kDa complex containing ZipA- EptA and an unidentified 24 kDa protein (PubMed:16079137), but it was shown later that there is no physical interaction between ZipA and EptA (PubMed:22304478). {ECO:0000305\|PubMed:16079137, ECO:0000305\|PubMed:22304478}.
Similarity:		Belongs to the ZipA family. {ECO:0000255\|HAMAP- Rule:MF_00509, ECO:0000305}.