cell-division inhibitor (septum placement), destabilizes Z ring placement
function
septum placement
product
cell-division inhibitor
Genomic Context
categories
[category|SW 1|Cellular processes] → [category|SW 1.1|Cell envelope and cell division] → [category|SW 1.1.8|Cell division] → [category|SW 1.1.8.1|The Min system][category|SW 4|Lifestyles] → [category|SW 4.3|Coping with stress] → [category|SW 4.3.2|Cell envelope stress proteins (controlled by SigM, V, W, X, Y)][category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins][SW|Categories] containing this gene/protein
[SW|cell division], [SW|cell envelope stress proteins (controlled by SigM, V, W, X, Y)], [SW|membrane proteins]This gene is a member of the following [SW|regulons]
[SW|SigH regulon], [SW|SigM regulon]Gene
Coordinates on the chromosome (coding sequence)
2,858,584 -> 2,859,264
Phenotypes of a mutant
a ''[protein|search|yvcL] [protein|search|minC]-[protein|search|minD]'' mutant grows poorly, and the cells are filamentous [Pubmed|24097947]The protein
Catalyzed reaction/ biological activity
The Min system prevents minicell formation adjacent to recently completed division sites by promoting the disassembly of the cytokinetic ring, thereby ensuring that cell division occurs only once per cell cycle [Pubmed|20352045]binds the C-terminal domain of [protein|search|FtsZ] to inhibit its polymerization [Pubmed|23577149]Protein family
minC family (according to Swiss-Prot)Structure
[PDB|1HF2] (from ''Thermotoga maritima'', 26% identity) [Pubmed|11350934][SW|Localization]
polar/ septal at the cell membrane [Pubmed|20566861]membrane binding/ polar localization depends on the proton motive force [Pubmed|20566861][SW|Interactions]
([protein|search|MinC]-[protein|search|MinD])-[protein|search|MinJ]-[SW|DivIVA] [Pubmed|20352045][protein|search|FtsZ] (C-terminal domain)-[protein|search|MinC] [Pubmed|23577149]Expression and Regulation
Operon
''[protein|search|radC]-[protein|search|mreB]-[protein|search|mreC]-[protein|search|mreD]-[protein|search|minC]-[protein|search|minD]'' [Pubmed|18179421]''[protein|search|mreB]-[protein|search|mreC]-[protein|search|mreD]-[protein|search|minC]-[protein|search|minD]'' [Pubmed|8459776]''[protein|search|minC]-[protein|search|minD]'' [Pubmed|8459776][SW|Sigma factor]
''[protein|search|radC]'': [protein|search|SigM] [Pubmed|18179421]''[protein|search|minC]'': [protein|search|SigH] [Pubmed|8459776]Regulation
expression is reduced in a [protein|search|SigV] mutant [Pubmed|21926231]constitutively expressed [Pubmed|23701187]Biological materials
Mutant
BSN375 (''[protein|search|minC]''::''aphA3'') (available in [SW|Leendert Hamoen]'s, [SW|Sven Halbedel]'s and [SW|Jörg Stülke]'s labs)two-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s labReferences
Reviews
19680248,19884039,24367361 Original Publications
8459776,19019154,1400224,10411726,15317782,20352045,18588879,19141479,20566861,20711458,24097947,18179421,22457634,23577149,21926231,23701187,24366721,11350934 
