Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. FloA and FloT function is partially redundant; double deletions have marked synthetic phenotypes (PubMed:20713508, PubMed:22753055, PubMed:25909364, PubMed:27362352). Flotillins are thought to be important factors in membrane fluidity, especially during periods of rapid growth in rich media (Probable). Whether specific proteins are associated with FMMs is controversial; in one study FloT rafts have been shown to include proteins involved in adaptation to stationary phase, while FloA-FloT rafts include proteins involved in differentation including sporulation, biofilm formation and DNA uptake competence (PubMed:25909364). Another (more finely resolved) study only showed association of NfeD2 with FloT rafts of all the proteins examined (PubMed:27362352). Involved in spatial organization of membranes, perhaps recruiting proteins to specific membrane regions (PubMed:23651456). Simultaneous overexpression of both FloA and FloT leads to defects in cell division and differentiation, in part caused by stabilization of FtsH and its subsequent increased ability to degrade proteins. Cells make more biofilm, are about half as long, have less EzrA and more frequent Z-rings (PubMed:24222488). Homooligomerizes (PubMed:25909364). Interacts with FloT (PubMed:23651456, PubMed:25909364, PubMed:26297017). Interacts with FtsH midcell (Probable). Interacts with PhoR, colocalizes with PhoR in FloA-only membrane rafts (PubMed:25909364). Present in detergent-resistant membrane (DRM) fractions, approximately 6 dynamic foci per cell; sometimes colocalizes with FloT in DRMs (PubMed:20713508, PubMed:22882210, PubMed:23651456). Found in discrete, highly mobile foci, rarely colocalizes with FloT (PubMed:22753055). At the septa colocalizes with FloT and FtsH (PubMed:22882210). Careful analysis gives an average of 13 FloA and 6 FloT foci per cell; FloA foci are smaller that FloT foci (PubMed:25909364). Another study shows FloA and FloT foci are similar in size, forming membrane assemblies of 85-110 nm, but FloA are more mobile than FloT foci. This study found no evidence of colocalization of FloA with FloT (PubMed:27362352). Few foci are seen on rich media, when cells are grown in minimal medium more foci are seen (at protein level) (PubMed:22753055). Constitutively expressed in rich and sporulation/biofilm-inducing media, not controlled by spo0A (at protein level) (PubMed:25909364). The last 95 residues are required for correct localization (PubMed:22753055). The C-terminus determines the oligomerization state of the protein; there are many small foci for FloA. Swapping with the C-terminus of FloT leads to fewer large foci (PubMed:25909364). N-terminally tagged, purified protein lacking the first 10 residues oligomerizes, with 12mer to about 50mer complexes found (PubMed:27362352). No effect on KinC activity, a double floT-floA deletion decreases the number of proteins in the DRM, blocks the ability of KinC to stimulate biofilm formation (PubMed:20713508). Single floA deletion has no change in FloT localization. Double floA-floT mutants have marked defects in cell morphology, motility, and transformation efficiency (PubMed:22753055). Single floA deletion sporulates less well. Double floA-floT deletion makes no biofilm, has greatly reduced FtsH, sporulates less than either single mutant (PubMed:22882210). Single mutation has a decrease in membrane fluidity, 25% decrease in protein secretion, double floT-floA deletion a stronger decrease in membrane fluidity and 35% decrease in protein secretion (PubMed:23651456). Double floA-floT deletion has reduced oligomerization of KinC (PubMed:26297017). Double floA-floT deletion cells are somewhat elongated, the site of cell wall synthesis is affected, increasing at division septa. The speed of MreB movement around the cell is significantly decreased in rich medium (PubMed:32662773). Belongs to the flotillin-like FloA family.