9.B.34 The Kinase/Phosphatase/Cyclic-GMP Synthase/Cyclic di-GMP Hydrolase (KPSH) Family

The KPSH family, is a heterogeneous group of multidomain proteins, each exhibiting a different set of domain combinations, suggesting differing catalytic and regulatory functions. Catalytic domains in these proteins include kinases, phosphatases, cyclic di-GMP synthetases and cyclic di-GMP hydrolases (KPSH). None of the members of the KPSH family have been functionally characterized, but the sequence similarity with characterized proteins and protein domains allowed functional predictions with a high degree of confidence (Mansour et al., 2007). The N-terminal 'transporter' domain has not been shown to have transport activity.


This family belongs to the BART Superfamily.
 

References:

Hu, L., C.J. Grim, A.A. Franco, K.G. Jarvis, V. Sathyamoorthy, M.H. Kothary, B.A. McCardell, and B.D. Tall. (2015). Analysis of the cellulose synthase operon genes, bcsA, bcsB, and bcsC in Cronobacter species: Prevalence among species and their roles in biofilm formation and cell-cell aggregation. Food Microbiol 52: 97-105.
Imai, T., S.J. Sun, Y. Horikawa, M. Wada, and J. Sugiyama. (2014). Functional reconstitution of cellulose synthase in Escherichia coli. Biomacromolecules 15: 4206-4213.
Mansour, N.M., M. Sawhney, D.G. Tamang, C. Vogl, and M.H. Saier, Jr. (2007). The bile/arsenite/riboflavin transporter (BART) superfamily. FEBS J. 274: 612-629.
Omadjela, O., A. Narahari, J. Strumillo, H. Mélida, O. Mazur, V. Bulone, and J. Zimmer. (2013). BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis. Proc. Natl. Acad. Sci. USA 110: 17856-17861.
Römling, U. and M.Y. Galperin. (2015). Bacterial cellulose biosynthesis: diversity of operons, subunits, products, and functions. Trends Microbiol. 23: 545-557.
Zogaj, X., M. Nimtz, M. Rohde, W. Bokranz, and U. Römling. (2001). The multicellular morphotypes of Salmonella typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix. Mol. Microbiol. 39: 1452-1463.
Examples:

TC#NameOrganismal TypeExample
9.B.34.1.1

The diguanylate cyclase (GGDEF domain-containing) protein with N-terminal "transporter" or "receptor" domain with 6 TMSs, Dge1 (Mansour et al., 2007).

Bacteria

Dge1 of Deinococcus geothermalis (Q1J0W6)

 
9.B.34.1.2

Transmembrane protein of 371 aas and 5 N-terminal TMSs. It is a positive regulator of cellulose biosynthesis, AdrA (Zogaj et al. 2001).

Proteobacteria

AdrA of E. coli

 
9.B.34.1.3

Putative diguanylate cyclase of 396 aas, with 6 N-terminal TMSs

Cyanobacteria

Diguanylate cyclase of Arthrospira platensis (Spirulina platensis)

 
9.B.34.1.4

Probable diguanylate cyclase of 564 aas with 1 N-terminal TMS and 1 central TMS, YedQ.  May play a regulatory role in cellulose synthase activity (Hu et al. 2015).

YedQ of E. coli

 
9.B.34.1.5

Diguanylate cyclase (GGDEF) domain-containing protein of 906 aas and 10 N-terminal TMSs.

DGC of Bacillus cereus

 
9.B.34.1.6

Putative diguanylate cyclase (GGDEF) with 272 aas and maybe 3 TMSs, two N-terminal, and one near the C-terminus.  This protein is encoded within an operon that also codes a putative phenylpropeneoid ABC-type transporter (TC# 3.A.1.4.11) and a putative phenylacetate-CoA ligase (Q6N8W5).

Putative diguanylate cyclase of Rhodopseudomonas palustris

 
9.B.34.1.7

Hybrid sensor histidine kinase/response regulator of 802 aas and 6 N-terminal TMSs with homology to members of family 9.B.34 in the TM domain.

SK-RR of Ahrensia sp.

 
9.B.34.1.8

EAL domain-containing protein of 878 aas and 6 N-terminal TM

EAL protein of Pseudomonas zhaodongensis

 
9.B.34.1.9

Diguanylate cyclase/phosphodiesterase of 806 aas and 10 N-terminal TMSs.

diGC of Mycolicibacterium rhodesiae

 
Examples:

TC#NameOrganismal TypeExample