| IED ID | IndEnz0002015397 |
| Enzyme Type ID | protease015397 |
| Protein Name |
Flotillin-like protein FloT Bacterial flotillin homolog YuaG |
| Gene Name | floT yuaG yuaH BSU31010 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MTMPIIMIIGVVFFLLIALIAVFITKYRTAGPDEALIVTGSYLGNKNVHVDEGGNRIKIVRGGGTFVLPVFQQAEPLSLLSSKLDVSTPEVYTEQGVPVMADGTAIIKIGGSIGEIATAAEQFLGKSKDDREQEAREVLEGHLRSILGSMTVEEIYKNREKFSQEVQRVASQDLAKMGLVIVSFTIKDVRDKNGYLESLGKPRIAQVKRDADIATAEADKETRIKRAEADKDAKKSELERATEIAEAEKINQLKMAEFRREQDTAKANADQAYDLETARARQQVTEQEMQVKIIERQKQIELEEKEILRRERQYDSEVKKKADADRYSVEQSAAAEKAKQLAEADAKKYSIEAMAKAEAEKVRIDGLAKAEAEKAKGETEAEVIRLKGLAEAEAKEKIAAAFEQYGQAAIFDMIVKMLPEYAKQAAAPLSNIDKITVVDTGGSGESSGANKVTSYATNLMSSLQESLKASSGIDVKEMLENFSGKGNVKQSINELTNEIKEAKTIQKSE |
| Enzyme Length | 509 |
| Uniprot Accession Number | O32076 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: 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. Another (more finely resolved) study only showed association of NfeD2 with FloT rafts of all the proteins examined (PubMed:25909364, PubMed:27362352). Aids homooligomerization of KinC and KinD but not KinB, may prevent incorrect hetero-association of the above kinases (PubMed:26297017). 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). Involved in spatial organization of membranes, perhaps recruiting proteins (e.g. NfeD2) to specific membrane regions (Probable) (PubMed:23651456). Plays a role in phosphorylation of master regulator Spo0A, an early sporulation event (PubMed:19383680). Plays a non-redundant role with dynamin-like protein A (dynA) in membrane dynamics and cell shape (PubMed:23249255). {ECO:0000269|PubMed:19383680, ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:24222488, ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:27362352, ECO:0000305|PubMed:22753055, ECO:0000305|PubMed:32662773}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Intramembrane (1); Motif (4); Mutagenesis (4); Region (3); Topological domain (2) |
| Keywords | Cell membrane;Cell shape;Membrane;Reference proteome;Repeat |
| Interact With | |
| Induction | INDUCTION: Transcription starts during stationary phase. Few foci are seen in exponential phase cells; the number of foci increases as cells enter stationary phase (at protein level) (PubMed:19383680, PubMed:23651456, PubMed:22753055). Few foci are seen on rich media, when cells are grown in minimal medium more foci are seen (at protein level) (PubMed:22753055). Expressed at low levels in rich media during exponential growth, more highly expressed in stationary phase on sporulation/biofilm-inducing media, activated by spo0A probably via AbrB (at protein level). Surfactin induces expression via spo0A (PubMed:25909364). {ECO:0000269|PubMed:19383680, ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25909364}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19383680, ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25909364, ECO:0000305|PubMed:25635948}. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352, ECO:0000305|PubMed:19383680}. Note=Tethered to the membrane by a hairpin loop that inserts into the cell membrane (PubMed:25635948). A few foci are seen on the cell membrane during exponential growth, more are seen as cells enter stationary phase. Restricted to the mother cell during sporulation. Foci form a spiral track on the cell membrane and move in the cell. Associated with high bouyancy, cardiolipin- and phosphatidylglycerol-rich membrane fractions, association is not obligatory (PubMed:19383680). Present in detergent-resistant membrane (DRM) fractions, approximately 6 dynamic foci per cell; colocalizes with KinC and sometimes with FloA in DRMs. Foci are lost when cells are treated with squalene synthase inhibitor zaragozic acid (PubMed:20713508). Found in discrete, highly mobile foci, often colocalizes with NfeD2 but rarely with FloA (PubMed:22753055). Forms discrete foci on the cell membrane, about 20% of foci are at the septal site. At the septa colocalizes with FloA and FtsH (PubMed:22882210, PubMed:23249255). Colocalizes with FtsX, OppA, SdhA and SecY in DRMs (PubMed:23651456). 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. FloA are more mobile than FloT foci and they do not overlap. This study found no evidence of colocalization of FloA with FloT, and nearly complete colocalization of FloT with NfeD2 (PubMed:27362352). {ECO:0000269|PubMed:19383680, ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25635948, ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 342..344; /note=EA repeat 1; /evidence=ECO:0000269|PubMed:25909364; MOTIF 357..360; /note=EA repeat 2; /evidence=ECO:0000269|PubMed:25909364; MOTIF 370..373; /note=EA repeat 3; /evidence=ECO:0000269|PubMed:25909364; MOTIF 390..394; /note=EA repeat 4; /evidence=ECO:0000269|PubMed:25909364 |
| Gene Encoded By | |
| Mass | 55,994 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |