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@ARTICLE{HaroMoreno:1025413,
      author       = {Haro-Moreno, Jose M. and López-Pérez, Mario and Alekseev,
                      Alexey and Podoliak, Elizaveta and Kovalev, Kirill and
                      Gordeliy, Valentin and Stepanauskas, Ramunas and
                      Rodriguez-Valera, Francisco},
      title        = {{F}lotillin-associated rhodopsin ({FA}rhodopsin), a
                      widespread paralog of proteorhodopsin in aquatic bacteria
                      with streamlined genomes},
      journal      = {mSystems},
      volume       = {8},
      number       = {3},
      issn         = {2379-5077},
      address      = {Washington, DC},
      publisher    = {American Society for Microbiology},
      reportid     = {FZJ-2024-02872},
      pages        = {e00008-23},
      year         = {2023},
      abstract     = {Microbial rhodopsins are found more than once in a single
                      genome (paralogs) often have different functions. We
                      screened a large dataset of open ocean single-amplified
                      genomes (SAGs) for co-occurrences of multiple rhodopsin
                      genes. Many such cases were found among Pelagibacterales
                      (SAR11), HIMB59, and the Gammaproteobacteria
                      Pseudothioglobus SAGs. These genomes always had a bona fide
                      proteorhodopsin and a separate cluster of genes containing a
                      second rhodopsin associated with a predicted flotillin
                      coding gene and have thus been named flotillin-associated
                      rhodopsins (FArhodopsins). Although they are members of the
                      proteorhodopsin protein family, they form a separate clade
                      within that family and are quite divergent from known
                      proton-pumping proteorhodopsins. They contain either DTT,
                      DTL, or DNI motifs in their key functional amino acids.
                      FArhodopsins are mainly associated with the lower layers of
                      the epipelagic zone. All marine FArhodopsins had the retinal
                      binding lysine, but we found relatives in freshwater
                      metagenomes lacking this key amino acid. AlphaFold
                      predictions of marine FArhodopsins indicate that their
                      retinal pocket might be very reduced or absent, hinting that
                      they are retinal-less. Freshwater FArhodopsins were more
                      diverse than marine ones, but we could not determine if
                      there were other rhodopsins in the genome due to the lack of
                      SAGs or isolates. Although the function of FArhodopsins
                      could not be established, their conserved genomic context
                      indicated involvement in the formation of membrane
                      microdomains. The conservation of FArhodopsins in diverse
                      and globally abundant microorganisms suggests that they may
                      be important in the adaptation to the twilight zone of
                      aquatic environments.},
      cin          = {IBI-7},
      ddc          = {570},
      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       = {37222519},
      UT           = {WOS:001026298700001},
      doi          = {10.1128/msystems.00008-23},
      url          = {https://juser.fz-juelich.de/record/1025413},
}