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Literature summary for 7.6.2.11 extracted from
- Functional characterization of murB-potABCD operon for polyamine uptake and peptidoglycan synthesis in Streptococcus suis (2018), Microbiol. Res., 207, 177-187 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| potABCD operon, genetic organization analysis, only one operon encoding a polyamine transport system (potABCD) is identified in the Streptococcus suis genome, sequence comparisons, the putative potABCD operon is co-transcribed with gene murB encoding UDP-N-acetylenolpyruvoylglucosamine reductase, EC 1.3.1.98, quantitative real-time PCR expression analysis of murB-potABCD operon in both wild-type and DELTApotA mutant strains. Recombinant expression of genes potA and potD, encoding PotA and PotD, in Escherichia coli strain BL21(DE3) as His-tagged proteins | Streptococcus suis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | putrescine does not inhibit the ATPase activity of PotA | Streptococcus suis | |
| spermidine | inhibits the ATPase activity of PotA | Streptococcus suis |  |
| spermine | strongly inhibits the ATPase activity of PotA | Streptococcus suis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Streptococcus suis | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Streptococcus suis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptococcus suis | A0A142UTH4 AND A0A0K2E5X6 AND G7SFQ8 AND A0A116LEI2 | genes potA, potB, potC, and potD encoding spermidine/putrescine import ATP-binding protein PotA, spermidine/putrescine ABC transporter permease PotB, spermidine/putrescine ABC transporter permease protein PotC, and spermidine/putrescine-binding periplasmic protein PotD; isolated from a diseased pig in Sichuan province of China | - |
| Streptococcus suis SC-19 | A0A142UTH4 AND A0A0K2E5X6 AND G7SFQ8 AND A0A116LEI2 | genes potA, potB, potC, and potD encoding spermidine/putrescine import ATP-binding protein PotA, spermidine/putrescine ABC transporter permease PotB, spermidine/putrescine ABC transporter permease protein PotC, and spermidine/putrescine-binding periplasmic protein PotD; isolated from a diseased pig in Sichuan province of China | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged PotA and PotD from Escherichia coli strain BL21(DE3) by nickel affinity chromataography | Streptococcus suis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + polyamine-[polyamine-binding protein][side 1] | - |
Streptococcus suis | ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1] | - |
? | |
| ATP + H2O + polyamine-[polyamine-binding protein][side 1] | - |
Streptococcus suis SC-19 | ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1] | - |
? | |
| ATP + H2O + spermidine-[polyamine-binding protein][side 1] | - |
Streptococcus suis | ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1] | - |
? | |
| ATP + H2O + spermidine-[polyamine-binding protein][side 1] | - |
Streptococcus suis SC-19 | ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1] | - |
? | |
| ATP + H2O + spermine-[polyamine-binding protein][side 1] | - |
Streptococcus suis | ADP + phosphate + spermine[side 2] + [polyamine-binding protein][side 1] | - |
? | |
| ATP + H2O + spermine-[polyamine-binding protein][side 1] | - |
Streptococcus suis SC-19 | ADP + phosphate + spermine[side 2] + [polyamine-binding protein][side 1] | - |
? | |
| additional information | PotD binding assays and ATPase activity assays of PotA are performed. A preference for extracellular polyamines in Streptococcus suis is identified as spermidine, spermine, putrescine in descending order, the uptake is competitive among the three | Streptococcus suis | ? | - |
? | |
| additional information | PotD binding assays and ATPase activity assays of PotA are performed. A preference for extracellular polyamines in Streptococcus suis is identified as spermidine, spermine, putrescine in descending order, the uptake is competitive among the three | Streptococcus suis SC-19 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 49000, recombinant His-tagged PotA, SDS-PAGE, x * 38000, recombinant His-tagged PotD, SDS-PAGE | Streptococcus suis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| polyamine transport system | - |
Streptococcus suis |
| PotA | - |
Streptococcus suis |
| potABCD | - |
Streptococcus suis |
| PotB | - |
Streptococcus suis |
| PotC | - |
Streptococcus suis |
| PotD | - |
Streptococcus suis |
| spermidine/putrescine ABC transporter permease | - |
Streptococcus suis |
| spermidine/putrescine ABC transporter permease I | - |
Streptococcus suis |
| Spermidine/putrescine ABC transporter permease protein | - |
Streptococcus suis |
| spermidine/putrescine import ATP-binding protein | - |
Streptococcus suis |
| spermidine/putrescine-binding periplasmic protein | - |
Streptococcus suis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Streptococcus suis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | - |
assay at | Streptococcus suis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Streptococcus suis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | PotA deletion disrupts normal peptidoglycan synthesis and hampers cell elongation. In contrast to the wild-type, the mutant DELTApotA exhibits elongated chain length and abnormal cell division morphology. Phenotypic changes are attributed to be the upregulation of genes involved in peptidoglycan (PG) synthesis and hydrolysis in DELTApotA. Cultivation of strain SC-19 in presence of excessive spermidine or spermine displays attenuated growth | Streptococcus suis |
| additional information | the putative potABCD operon is co-transcribed with gene murB encoding UDP-N-acetylenolpyruvoylglucosamine reductase, EC 1.3.1.98, also involved in peptidoglycan synthesis | Streptococcus suis |
| physiological function | the polyamine transport system PotABCD in Streptococcus suis can uptake polyamines preferably spermidine and spermine. Spermidine and putrescine have been found to be constituents of the cell wall peptidoglycan, these molecules maintain the integrity of the cell surface structure and normal cell growth. The known de novo synthesis pathway is not observed in strain SC-19 according to the genome of the strain. Regulatory roles of polyamine on polyamine transport and peptidoglycan (PG) synthesis. Polyamines function not only as feedback regulators of PotA by inhibiting PotA activity but also as regulators on potABCD and genes involved in PG synthesis. The binding of high-concentration spermidine to PotA decreases the ATPase activity and inhibits polyamine transport. PotD can downregulate the transcription of the potABCD operon. Thus, both receptor and ligand can function as feedback regulators of polyamine transport | Streptococcus suis |
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