Protein: Dynamin-like protein A (DynA) (P54159)
Organism: Bacillus subtilis (strain 168)
Function: Mediates lipid mixing of vesicles and full mixing of their contents in the absence and presence of GTP. Tethers and mixes small vesicles better than larger ones, indicating a curvature preference. GTP slows down DynA-mediated lipid fusion, perhaps controlling its activity. Prefers phospholipid composition close to the B.subtilis membrane; requires phosphatidylglycerol for fusion has no activity on pure phosphatidylethanolamine vesicles. Regulates membrane lipid diffusion. Required to prevent membrane damage when exposed to low levels of membrane-damaging antibiotics or to bacteriophage. Probably surveys the cell membrane for stress; localizes to sites of membrane damage (treatment with nisin) and forms foci in cells treated with pore-forming compounds (CCCP). May assist membrane repair, possibly by membrane tethering and fusion. Probably functions both in early and late cell division, affects the proper formation of the FtsZ ring. Plays a non-redundant role with flottilin (floT) in membrane dynamics and cell shape. Probably able to bend membranes. Tethers liposomes and mediates their fusion; this does not require GTPase activity or the presence of GTP. Both GTPase domains (dynamin-type G) are required for GTPase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21205012, ECO:0000269|PubMed:23060960, ECO:0000305|PubMed:26530236}; Peripheral membrane protein {ECO:0000305}. Note=Found at the division septum; in the absence of minJ dispersed along membrane. Associates with the cell membrane via the D1 domain, D2 does not associate with membranes (PubMed:21205012, PubMed:23060960). In growing cells forms foci at midcell, colocalizes with FtsZ. Membrane localized in non-growing cells (PubMed:23249255). Localized uniformly along cell membrane where it is highly dynamic, DynA localizes to regions of membrane deformation upon nisin treatment and remains at those sites. Localizes into foci upon membrane potential dissipation (CCCP treatment, forms membrane pores) (PubMed:26530236). {ECO:0000269|PubMed:21205012, ECO:0000269|PubMed:23060960, ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:26530236}.
Interaction partners:
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS9
- Uncharacterized protein YpbS
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS15
- Protein YwpG
- Small ribosomal subunit protein uS5
- UPF0603 protein YdjH
Sequence:
MTDQNRKELLHKTGELYKQFIENQDEQRAAKLAAVMKKAADEEVYIAFTGHYSAGKSSLLNCLLMENILPTSPIPTSANLVVIRNGEKRVRLHTTDGACAELEGTYQKDKVQQYCKDGEQIESVEIFDRYTEIDSGVAYIDTPGIDSTDDAHFLSAASILHQADALFYVVHYNHVHAEENVKFLRSIKESIPNVYFIVNQIDRHDETETKFGDYQAQVEEMLCNEGISREALYFTSVTEPDHPFNQMGALREELSRIEQQSKSNMQALTEQKVRNLLKEHTEMLKKDETGAPSFAEQLNIHTGLVQSLRDQLDEAEKQMTEAEKRMQEEINRILKNANLTPFEMRELAAAFLESQEPSFKTGFFFSKAKTAQERDKRRNAFFSDVAKRTEAEADWHMIDTLHKLAKVFDVYTAESEKLIQAYRTPLDISIIEHAVKHGAAFSSEYVLQYTKDLAELIRKEAKREAADIIKVLSAMVKERVSKDVQTINDRLVQESEKLVFLQEQARLENNAREKTDRLWAIWEEESACPMHIDTEWFKSKKTRVAAPEQKQGRSQLTAQPMPKSEIKMEQEMPLQDQIKRFYTLSDILGECSMLLKQTSAFRERVKRLEERKFTLALFGGFSSGKSSFANALVGERVLPSSPTPTTATINKITKPINGNLNKTANVVFKTEDDLTAEILQLTGIPKEPAGRSFTEKWEKAVKKNRLQEEHVKLISNFLLAYEKYQQYIQEQKKLTIPLSELKPYVAEETTACAVKEVTVYYTCPLTEKGITIVDTPGASSMNKRHTELAFQYIKDADAFFYMTYYQHSFSKGDRSFLRKLGLVKESLSMDKMFFIINAADLAKDKTELETVTDYVSAELVKEGVYEPQLFTVSSKEELVGKPESFYNQFSKVRKHLDRFIEVDVKKASAAQLSSEADKLCETVFQLHQSQHQSREEKEAQKQCLMLSFERTAADIEKRRNSKTIIEKVKKDTREQLYHIAQRLSYFANDLLKSAFHPGLQNGDWKKNVSKAMTTALHEYLFEYIQEIKTLDVRMSGFIERHINEEWLDHFQKTLNEDGYFSVYAGDQHSNGIQLKEVEPEIEERAFEQELKEIKSPKQFFEQKGKATFIEAVRMKLTKITEAWIKNEEESLISHYTAHLRRLQEDMGEKAIAQITDQKETYLRGYAEGEHAKEIEMAYQACISWKNSDNTIKM