Biological Nitrogen Removal Database

A manually curated data resource for microbial nitrogen removal


Detailed information

Microorganism

Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)

Taxonomy

  • Phylum : Stenosarchaea group
  • Class : Halobacteria
  • Order : Haloferacales
  • Family : Haloferacaceae
  • Genus : Haloferax

Isolation Source

nan

Enzyme Name

Chaperone protein

  • Encoding Gene:narJ
  • DNA Size:321908 bp
  • Nucleotide FASTA sequence: Link

  • UniProt I.D: I3R9M6

Protein Information

  • Pro_GenBank I.D: AFK20936.1

  • Length:242 aa
  • Protein FASTA_sequence: Link

Information about Article

  • Reference:Cai et al., 2012
  • Title:Identification of the haloarchaeal phasin (PhaP) that functions in polyhydroxyalkanoate accumulation and granule formation in Haloferax mediterranei
  • Pubmed ID:22247127.0
  • Pubmed link: Link

  • Full research link: Link

  • Abstract:The polyhydroxyalkanoate (PHA) granule-associated proteins (PGAPs) are important for PHA synthesis and granule formation, but currently little is known about the haloarchaeal PGAPs. This study focused on the identification and functional analysis of the PGAPs in the haloarchaeon Haloferax mediterranei. These PGAPs were visualized with two-dimensional gel electrophoresis (2-DE) and identified by matrix-assisted laser desorption ionization-tandem time of flight mass spectrometry (MALDI-TOF/TOF MS). The most abundant protein on the granules was identified as a hypothetical protein, designated PhaP. A genome-wide analysis revealed that the phaP gene is located upstream of the previously identified phaEC genes. Through an integrative approach of gene knockout/complementation and fermentation analyses, we demonstrated that this PhaP is involved in PHA accumulation. The ΔphaP mutant was defective in both PHA biosynthesis and cell growth compared to the wild-type strain. Additionally, transmission electron microscopy results indicated that the number of PHA granules in the ΔphaP mutant cells was significantly lower, and in most of the ΔphaP cells only a single large granule was observed. These results demonstrated that the H. mediterranei PhaP was the predominant structure protein (phasin) on the PHA granules involved in PHA accumulation and granule formation. In addition, BLASTp and phylogenetic results indicate that this type of PhaP is exclusively conserved in haloarchaea, implying that it is a representative of the haloarchaeal type PHA phasin.