Protein Domain : IPR010127

Type:  Family Name:  Phasin, subfamily 1
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. This entry describes a group of phasins associated with polyhydroxyalkanoate (PHA) inclusions, the most common of which consist of polyhydroxybutyrate (PHB). However, the member from Magnetospirillum sp.(strain AMB-1) is called a magnetic particle membrane-specific GTPase. Short Name:  Phasin_subfam-1
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0 Child Features

0 Contains

1 Cross References

Identifier
TIGR01841

0 Found In

0 GO Annotation

0 Ontology Annotations

0 Parent Features

3 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
31112.m000023 B9TMG1 PAC:16824818 Ricinus communis 147  
51811.m000024 B9TN73 PAC:16828453 Ricinus communis 122  
59090.m000017 B9TQA9 PAC:16829218 Ricinus communis 143  

3 Publications

First Author Title Year Journal Volume Pages PubMed ID
            17965215
            18223073
            15256572