Biological Nitrogen Removal Database

A manually curated data resource for microbial nitrogen removal


Detailed information

Microorganism

Laribacter hongkongensis HLHK9

Taxonomy

  • Phylum : Proteobacteria
  • Class : Betaproteobacteria
  • Order : Neisseriales
  • Family : Chromobacteriaceae
  • Genus : Laribacter

Isolation Source

Host: human - immunocompetent patient with severe gastroenteritis

Enzyme Name

Periplasmic nitrate reductase, electron transfer subunit

  • Encoding Gene:NapB
  • DNA Size:3169329 bp
  • Nucleotide FASTA sequence: Link

  • UniProt I.D: C1D9G6

Protein Information

  • Pro_GenBank I.D: ACO75068.1

  • Length:146 aa
  • Protein FASTA_sequence: Link

Information about Article

  • Reference:Woo et al., 2009
  • Title:The complete genome and proteome of Laribacter hongkongensis reveal potential mechanisms for adaptations to different temperatures and habitats
  • Pubmed ID:19283063.0
  • Pubmed link: Link

  • Full research link: Link

  • Abstract:Laribacter hongkongensis is a newly discovered Gram-negative bacillus of the Neisseriaceae family associated with freshwater fish-borne gastroenteritis and traveler's diarrhea. The complete genome sequence of L. hongkongensis HLHK9, recovered from an immunocompetent patient with severe gastroenteritis, consists of a 3,169-kb chromosome with G+C content of 62.35%. Genome analysis reveals different mechanisms potentially important for its adaptation to diverse habitats of human and freshwater fish intestines and freshwater environments. The gene contents support its phenotypic properties and suggest that amino acids and fatty acids can be used as carbon sources. The extensive variety of transporters, including multidrug efflux and heavy metal transporters as well as genes involved in chemotaxis, may enable L. hongkongensis to survive in different environmental niches. Genes encoding urease, bile salts efflux pump, adhesin, catalase, superoxide dismutase, and other putative virulence factors-such as hemolysins, RTX toxins, patatin-like proteins, phospholipase A1, and collagenases-are present. Proteomes of L. hongkongensis HLHK9 cultured at 37 degrees C (human body temperature) and 20 degrees C (freshwater habitat temperature) showed differential gene expression, including two homologous copies of argB, argB-20, and argB-37, which encode two isoenzymes of N-acetyl-L-glutamate kinase (NAGK)-NAGK-20 and NAGK-37-in the arginine biosynthesis pathway. NAGK-20 showed higher expression at 20 degrees C, whereas NAGK-37 showed higher expression at 37 degrees C. NAGK-20 also had a lower optimal temperature for enzymatic activities and was inhibited by arginine probably as negative-feedback control. Similar duplicated copies of argB are also observed in bacteria from hot springs such as Thermus thermophilus, Deinococcus geothermalis, Deinococcus radiodurans, and Roseiflexus castenholzii, suggesting that similar mechanisms for temperature adaptation may be employed by other bacteria. Genome and proteome analysis of L. hongkongensis revealed novel mechanisms for adaptations to survival at different temperatures and habitats.