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@ARTICLE{Gushchin:894236,
      author       = {Gushchin, Ivan and Aleksenko, Vladimir A. and Orekhov,
                      Philipp and Goncharov, Ivan M. and Nazarenko, Vera V. and
                      Semenov, Oleg and Remeeva, Alina and Gordeliy, Valentin},
      title        = {{N}itrate- and {N}itrite-{S}ensing {H}istidine {K}inases:
                      {F}unction, {S}tructure, and {N}atural {D}iversity},
      journal      = {International journal of molecular sciences},
      volume       = {22},
      number       = {11},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2021-03116},
      pages        = {5933 -},
      year         = {2021},
      abstract     = {Under anaerobic conditions, bacteria may utilize nitrates
                      and nitrites as electron acceptors. Sensitivity to nitrous
                      compounds is achieved via several mechanisms, some of which
                      rely on sensor histidine kinases (HKs). The best studied
                      nitrate- and nitrite-sensing HKs (NSHKs) are NarQ and NarX
                      from Escherichia coli. Here, we review the function of
                      NSHKs, analyze their natural diversity, and describe the
                      available structural information. In particular, we show
                      that around 6000 different NSHK sequences forming several
                      distinct clusters may now be found in genomic databases,
                      comprising mostly the genes from Beta- and
                      Gammaproteobacteria as well as from Bacteroidetes and
                      Chloroflexi, including those from anaerobic ammonia
                      oxidation (annamox) communities. We show that the
                      architecture of NSHKs is mostly conserved, although proteins
                      from Bacteroidetes lack the HAMP and GAF-like domains yet
                      sometimes have PAS. We reconcile the variation of NSHK
                      sequences with atomistic models and pinpoint the structural
                      elements important for signal transduction from the sensor
                      domain to the catalytic module over the transmembrane and
                      cytoplasmic regions spanning more than 200 Å.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34072989},
      UT           = {WOS:000660135300001},
      doi          = {10.3390/ijms22115933},
      url          = {https://juser.fz-juelich.de/record/894236},
}