Related Experiment Video
Updated: Jul 30, 2026

Assaying for Inorganic Polyphosphate in Bacteria
Published on: January 21, 2019
Manganese-dependent protein O-phosphatases in prokaryotes and their biological functions
1Environmental Microbiology Group, Pacific Northwest National Laboratory, 902 Battelle Blvd., P.O.Box 999, MSIN: P7-50, Richland, WA 99352, USA. Liang.Shi@pnl.gov
Abstract:
During the past decade, numerous Mn2+-dependent protein serine, threonine and/or tyrosine phosphatases (O-phosphatases) from prokaryotes have been characterized. Based on their amino acid sequences, they belong to PPP, PPM or PHP superfamilies. Both the PPP and PPM families of protein phosphatases are metalloenzymes which active centers contain two metal ions that function as cofactors. Results from sequence analysis also suggest that PHP family protein phosphatase is a metalloenzyme. The identified functions for PPP family protein phosphatases from different prokaryotic organisms include regulation of stress-response, nitrogen fixation and vegetative growth. At least one phosphatase, PrpB from Escherichia coli, is also implicated in bacterial pathogenesis. Prokaryotic PPM family protein phosphatases are involved in controlling spore formation, stress-response, cell density during stationary phase, carbon and nitrogen assimilation, vegetative growth, development of fruiting bodies and cell segregation. The function of CpsB, a PHP family protein tyrosine phosphatase from Streptococcus pneumonia, is to regulate biosynthesis of capsular polysaccharide, an important virulence determinant. Thus, this group of functionally diverse protein phosphatases plays an important role in prokaryotes. Discovery of Mn2+-dependent prokaryotic protein O-phosphatases and their functions also contributes to new insight into Mn2+ homeostasis and many roles played by Mn2+ and protein O-phosphorylation in prokaryotic cells.
Insights
Numerous Mn2+-dependent protein phosphatases (O-phosphatases) in prokaryotes, belonging to PPP, PPM, and PHP families, regulate vital cellular processes. Their discovery offers new insights into manganese homeostasis and protein phosphorylation in bacteria.
Area of Science:
- Biochemistry
- Molecular Biology
- Microbiology
Background:
- Prokaryotic protein phosphatases (O-phosphatases) are crucial enzymes dependent on Mn2+ cofactors.
- These phosphatases are classified into PPP, PPM, and PHP superfamilies based on sequence homology.
- Many prokaryotic O-phosphatases are metalloenzymes, utilizing metal ions in their active sites.
Purpose of the Study:
- To review and characterize the diverse functions of Mn2+-dependent protein phosphatases in prokaryotes.
- To highlight the roles of PPP, PPM, and PHP families in various cellular processes.
- To underscore the significance of these enzymes in understanding prokaryotic physiology and Mn2+ homeostasis.
Main Methods:
- Sequence analysis to classify protein phosphatases into superfamilies (PPP, PPM, PHP).
- Literature review of characterized prokaryotic O-phosphatases and their identified functions.
- Functional annotation based on experimental data and sequence homology.
Main Results:
- PPP family phosphatases regulate stress response, nitrogen fixation, and growth.
- PPM family phosphatases are involved in spore formation, stress response, and cell division.
- PHP family phosphatases, like CpsB, regulate virulence factors such as capsular polysaccharide synthesis.
Conclusions:
- Mn2+-dependent protein O-phosphatases are functionally diverse and essential in prokaryotes.
- These enzymes play critical roles in stress response, growth, development, and virulence.
- Their study provides valuable insights into Mn2+ homeostasis and protein phosphorylation in prokaryotic cells.
Related Concept Videos
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Microbes and Other Elemental Cycles

