| http://purl.uniprot.org/proteomes/UP000006469 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Proteome |
| http://purl.uniprot.org/proteomes/UP000006469 | http://www.w3.org/2000/01/rdf-schema#comment | "Polyhydroxyalkanoates (PHAs) are biodegradable polyesters present in most genera of bacteria and in Halobacteriaceae members of archaea. PHAs usually accumulate when cells are cultivated in an environment with an excess of carbon sources and limited nitrogen, phosphorus, or oxygen. Serving as carbon and energy storage compounds, PHAs are often found in the cytoplasm as insoluble inclusions that are also known as PHA granules. Many proteins coated onto PHA granules (PHA granule-associated proteins (PGAPs)) have been shown to be responsible for PHA synthesis and granule formation. The major proteins present on PHA granules, the phasins (PhaPs), constitute approximately 5% (wt/wt) of total cellular proteins. In addition to their main roles in preventing PHA granules from aggregating and in preventing the nonspecific attachment of other proteins to PHA granules, phasins are proposed to be involved in the regulation of PHA synthesis, PHA degradation, PHA granule size control, the formation of networks on the PHA granule surface, and even the distribution of PHA granules during cell division, a dramatic role displayed by phasin PhaF and the phasin-like PhaM. Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) is an extremely halophilic, poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer archaeon isolated from seawater evaporation ponds near Alicante, Spain. It exhibits remarkable metabolic efficiency and genome stability at high salt concentrations and thus has served as a good model for haloarchaeal physiology and metabolism studies for several decades. H. mediterranei is capable of accumulating poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV) from many cheap carbon sources. It possesses 2 key enzymes (PhaEC and PhaB) and a structure protein (PhaP) involved in PHBV biosynthesis. (Adapted from PMID: 22843593 & 22247127)."xsd:string |
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| http://purl.uniprot.org/proteomes/UP000006469 | http://www.w3.org/2000/01/rdf-schema#seeAlso | http://purl.uniprot.org/proteomes/UP000006469#source |
| http://purl.uniprot.org/proteomes/UP000006469 | http://purl.uniprot.org/core/organism | http://purl.uniprot.org/taxonomy/523841 |
| http://purl.uniprot.org/proteomes/UP000006469 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22843593 |
| http://purl.uniprot.org/proteomes/UP000006469 | http://www.w3.org/2004/02/skos/core#closeMatch | http://purl.uniprot.org/proteomes/UP000006469#cpd |
| http://purl.uniprot.org/proteomes/UP000006469 | http://purl.org/dc/terms/modified | "2022-06-23"xsd:date |
| http://purl.uniprot.org/proteomes/UP000006469 | http://www.w3.org/2004/02/skos/core#narrower | http://purl.uniprot.org/proteomes/UP000006469#Chromosome |
| http://purl.uniprot.org/proteomes/UP000006469 | http://www.w3.org/2004/02/skos/core#narrower | http://purl.uniprot.org/proteomes/UP000006469#Plasmid%20pHM500 |
| http://purl.uniprot.org/proteomes/UP000006469 | http://www.w3.org/2004/02/skos/core#narrower | http://purl.uniprot.org/proteomes/UP000006469#Plasmid%20pHM300 |
| http://purl.uniprot.org/proteomes/UP000006469 | http://www.w3.org/2004/02/skos/core#narrower | http://purl.uniprot.org/proteomes/UP000006469#Plasmid%20pHM100 |
| http://purl.uniprot.org/proteomes/UP000006469 | http://busco.ezlab.org/schema#has_score | http://purl.uniprot.org/proteomes/UP000006469#busco |
| http://purl.uniprot.org/proteomes/UP000006469 | http://purl.uniprot.org/core/panproteome | http://purl.uniprot.org/proteomes/UP000008243 |
| http://purl.uniprot.org/proteomes/UP000006469 | http://purl.uniprot.org/core/strain | http://purl.uniprot.org/proteomes/UP000006469#ATCC%2033500%20%2F%20DSM%201411%20%2F%20JCM%208866%20%2F%20NBRC%2014739%20%2F%20NCIMB%202177%20%2F%20R-4 |
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