Structure and distribution of pentapeptide repeats in bacteria

Protein Sci. 1998 Jun;7(6):1477-80. doi: 10.1002/pro.5560070625.


We report the discovery of a novel family of proteins, each member contains tandem pentapeptide (five residue) repeats, described by the motif A(D/N)LXX. Members of this family are both membrane bound and cytoplasmic. The function of these repeats is uncertain, but they may have a targeting or structural function rather than enzymatic activity. This family is most common in cyanobacteria, suggesting a function related to cyanobacterial-specific metabolism. Although no experimental information is available for the structure of this family, it is predicted that the tandem pentapeptide repeats will form a right-handed beta-helical structure. A structural model of the pentapeptide repeats is presented.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Cyanobacteria / chemistry*
  • HSP70 Heat-Shock Proteins / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Oligopeptides / chemistry*
  • Protein Kinases / chemistry
  • Protein Structure, Secondary
  • Repetitive Sequences, Nucleic Acid*


  • Bacterial Proteins
  • HSP70 Heat-Shock Proteins
  • Oligopeptides
  • Protein Kinases