Structure and distribution of pentapeptide repeats in bacteria.
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.
Bateman
A
A
Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom. agb@sanger.ac.uk
Murzin
A G
AG
Teichmann
S A
SA
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D000458:Cyanobacteria / Q000737:chemistry*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D011494:Protein Kinases / Q000737:chemistry; D017433:Protein Structure, Secondary; D012091:Repetitive Sequences, Nucleic Acid
D001426:Bacterial Proteins; D018840:HSP70 Heat-Shock Proteins; D009842:Oligopeptides; D011494:Protein Kinases