8.A.8 The Phosphotransferase System HPr (HPr) Family

The HPr family consists of bacterial and archaeal proteins, all of which function as phosphoryl transfer proteins. They are energy-coupling constituents of the phosphotransferase system (PTS) (TC #4.A.1-4.A.7) which catalyzes sugar uptake via a group translocation mechanism. HPr proteins are not known to be homologous to any non-PTS proteins. The E. coli genome encodes five HPr paralogues. The functions of several of these proteins are known. They function in PTS-related regulatory capacities. 

Ruminiclostridium cellulolyticum has incomplete PTS components (Xu et al. 2023). Inactivation of the HPr homolog reduced rather than increased carbohydrate utilization. In addition to regulating transcriptional profiles, PTS associated CcpA (Catabolite Control Protein A) homologs diverged from previously described CcpA with varied metabolic relevance and distinct DNA binding motifs. The DNA binding of CcpA homologs is independent of HPr homologs, which are determined by structural changes at the interfaces of CcpA homologs. Thus, results support functional and structural diversification of PTS components in metabolic regulation and bring novel understanding of regulatory mechanisms of incomplete PTSs in cellulose-degrading clostridia (Xu et al. 2023).


 

References:

Araki N., Suzuki T., Miyauchi K., Kasai D., Masai E. and Fukuda M. (201). Identification and characterization of uptake systems for glucose and fructose in Rhodococcus jostii RHA1. J Mol Microbiol Biotechnol. 20(3):125-36.
Parche, S., R. Schmid, and F. Titgemeyer. (1999). The phosphotransferase system (PTS) of Streptomyces coelicolor identification and biochemical analysis of a histidine phosphocarrier protein HPr encoded by the gene ptsH. Eur J Biochem 265: 308-317.
Pickl A., Johnsen U. and Schonheit P. (2012). Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase. J Bacteriol. 194(12):3088-97.
Postma, P.W., J.W. Lengeler and G.R. Jacobson (1993). Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57: 543-594.
Reizer, J., C. Hoischen, A. Reizer, T.N. Pham and M.H. Saier, Jr. (1993). Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate:sugar phosphotransferase system. Prot. Sci. 2: 506-521.
Titgemeyer, F., J. Walkenhorst, J. Reizer, M.H. Stuiver, X. Cui, and M.H. Saier, Jr. (1995). Identification and characterization of phosphoenolpyruvate:fructose phosphotransferase systems in three Streptomyces species. Microbiology 141(Pt1): 51-58.
Xu, T., X. Tao, H. He, M.L. Kempher, S. Zhang, X. Liu, J. Wang, D. Wang, D. Ning, C. Pan, H. Ge, N. Zhang, Y.X. He, and J. Zhou. (2023). Functional and structural diversification of incomplete phosphotransferase system in cellulose-degrading clostridia. ISME J 17: 823-835.
Examples:

TC#NameOrganismal TypeExample
8.A.8.1.1HPr of the PTS Bacteria HPr of E. coli (P0AA04)
 
8.A.8.1.2

HPr of the PTS (Araki et al., 2011)

Bacteria

HPr of Rhodococcus jostii (Q0S1N3)

 
8.A.8.1.3

PTS phosphocarrier protein, HPr (based on homology)

Archaea

HPr of Haloterrigena turkmenica (D2RXA6)

 
8.A.8.1.4

Phosphocarrier Protein, HPr. (functions with 4.A.2.1.15; Pickl et al., 2012).

Archaea

HPr of Haloferax volcanii (D4GYE3)

 
8.A.8.1.5

Phosphotransferase system, phosphocarrier protein HPr of 89 aas.  This protein is encoded in the same operon with an Enzyme I (TC# 8.A.7.1.5) and the IIC and IID genes of a mannose-type PTS system (TC# 4.A.6.1.20).

HPr of Caldithrix abyssi

 
8.A.8.1.6

HPr of an archaeal PTS of the mannose (Man) type; 90 aas.

HPr of Thermofilum pendens

 
8.A.8.1.7

The phosphocarrierprotein of the PTS, HPr (PtsH) of 93 aas. In this organism and another Streptomyces species, S. lividans, HPr and Enzyme I are inducible by fructose (Titgemeyer et al. 1995), and they comprise a complete fructose phosphorylation and transport system (Parche et al. 1999). All pts related genes present in the S. coelicolor genome have been identifed, and in addition to the Fructose PTS described above, there are several other PTS enzyme II complexes, that transport other sugars (Parche et al. 1999) including N-acetylglucosamine which serves as a sensing device as well as a transporter/kinase for N-acetylglucosamine (see TC# 4.A.1.1.20) (Nothaft et al. 2010).

HPr of Streptomyces coelicolor