TABLE 1.
PTS component | Non-PTS phosphorylation/interaction partner(s) | Phosphorylation or interaction | Effect(s) of phosphorylation or interaction |
---|---|---|---|
EI (E. coli) | CheA, chemotaxis protein | Interaction | Stimulates CheA autophosphorylation |
P∼EI (B. subtilis) | CheA, chemotaxis protein | Interaction | Inhibits CheA autophosphorylation |
HPr (E. coli) | Glycogen phosphorylase | Interaction | Stimulates glycogen phosphorylase activity |
P∼His-HPr (E. coli) | Glycogen phosphorylase | Interaction | Prevents binding of HPr to glycogen phosphorylase |
P∼His-HPr | Antiterminators, BglG, SacY, LicT, etc.a | Phosphorylation in PRD2 | Stimulates antitermination,b alternate CCR mechanism |
Transcription activators, LevR-like | Phosphorylation in the EIIAMan domain | Stimulates transcription, alternate CCR mechanism | |
Transcription activators, MtlR-like | Phosphorylation in PRD2 | Stimulates transcription, alternate CCR mechanism | |
Transcription activators, LicR-like | Phosphorylation in PRD1 and PRD2 | Stimulates transcription, alternate CCR mechanism | |
P∼His-HPr (firmicutes) | Glycerol kinase GlpK | Phosphorylation, His in the N-terminal half | Stimulates GlpK activity, inducer exclusion |
LacS, RafP; transporters for lactose, raffinose | Phosphorylation in the EIIAGlc domain | Stimulates substrate/galactose exchange | |
P-Ser-HPr (firmicutes) | CcpA | Interaction | CCR or CCA, catabolite corepressor |
Non-PTS transporters for maltose, ribose, etc. | Interaction | Inducer exclusionc | |
RbsR | Interaction | Physiological role not yet established | |
P-Ser-Crh (bacilli) | CcpA | Interaction | CCR or CCA, catabolite corepressor |
EIIAGlc (enterobacteria) | Non-PTS transporters LacY, MalK, MelB | Interaction | Inducer exclusion |
Glycerol kinase, GlpK | Interaction with the C-terminal domain | Inducer exclusion | |
Fermentation respiration switch protein, FrsA | Interaction | Probably causes increased respiration | |
P∼EIIAGlc (enterobacteria) | Adenylate cyclase | Interaction | CCR, activation of adenylate cyclased |
P∼EIIADha | DhaL, L subunit of dihydroxyacetone kinase | Phosphoryl transfer | ADP bound to DhaL is converted into ATP |
EIIBGlc (enterobacteria) | Mlc | Interaction | Derepression of genes of the Mlc regulon |
P∼EIIBs, Glc/Sac/Lac class | Antiterminators, BglG, SacY, LicT, etc.a | Phosphorylation in PRD1e | Inhibits antitermination, induction mechanism |
P∼EIIBs, Man/Lac class | Transcription activators, LevR-like | Phosphorylation in PRD2e | Inhibits transcription, induction mechanism |
P∼EIIBs, Mtl/Gut class | Transcription activators, MtlR-like | Phosphorylation in the EIIAMtl domaine | Inhibits transcription, induction mechanism |
P∼EIIBs, Lac/Cel class | Transcription activators, LicR-like | Phosphorylation in the EIIAMtl domaine | Inhibits transcription, induction mechanism |
For a more detailed summary of well-studied antiterminators, see Table 4.
Certain antiterminators (such as SacY and GlcT of B. subtilis) are phosphorylated in vitro by P∼His-HPr in PRD2, but their activity is not stimulated by this modification.
An interaction of P-Ser-HPr with the maltose or ribose transport systems in L. casei and L. lactis has so far not been demonstrated but is suggested from genetic experiments.
An additional cellular factor seems to be necessary for the activation of adenylate cyclase by P∼EIIAGlc (632).
It is not clear whether phosphorylation of the antiterminators/transcription activators occurs via P∼His-HPr and P∼EIIBs stimulate only the phosphoryl transfer or whether the phosphoryl group is transferred from P∼EIIBs to the antiterminators/transcription activators. It is possible that both modes of regulation exist.