| Primary Identifier | IPR014176 | Type | Family |
| Short Name | Phasin_subfam-3 |
| description | Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granules by many bacteria under unfavorable conditions, enhancing their fitness and stress resistance []. The layer of phasins stabilises the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. For example, in Ralstonia eutropha (strain ATCC 17699/H16/DSM 428/Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)), the major surface protein of polyhydroxybutyrate (PHB) granules is phasin PhaP1(Reu), which occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels [, ]. These four phasins lack a highly conserved domain but share homologous hydrophobic regions. Members of this entry are encoded in polyhydroxyalkanoic acid storage system regions in a number of Vibrio species, including Vibrio cholerae V52, Photobacterium profundum SS9, Acinetobacter sp., and Aeromonas hydrophila. Members appear distantly related to the phasin family, see: and . |
