EC Number   |
General Information |
Reference |
|---|
   7.6.2.11 | evolution |
SapABCDF is specifically distributed within gamma-proteobacteria |
-, 751075 |
| 7.6.2.11 | malfunction |
deletion of sapBCDF significantly decreases putrescine levels in the cell culture supernatant, and the DELTAsapBCDF strain does not facilitate uptake of putrescine from the culture supernatant. Complementation of the deletion mutant with the sapBCDF genes restores putrescine levels in the culture supernatant. Putrescine concentration of the culture supernatant is not influenced by DELTAsapA but is affected by DELTAsapBCDF. The Escherichia coli DELTAsapBCDF strain does not show affected resistance to antimicrobial peptide LL-37t |
-, 751075 |
| 7.6.2.11 | malfunction |
inactivation of the gene cluster potADB, encoding a polyamine ABC transporter disrupted diazotrophic growth, corroborates the importance of polyamine homeostasis in Nostoc sp. PCC 7120 |
-, 751585 |
| 7.6.2.11 | 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 |
-, 751493 |
| 7.6.2.11 | metabolism |
the enzyme complex SapBCDF exports putrescine from Escherichia coli cells to the culture supernatant, which is the natural function of the SapBCDF proteins, while PotABCD is a spermidine transporter of the ABC transporter family that takes up putrescine with lower affinity. Mechanism of polyamine export from bacterial cells to the intestinal lumen. PuuP is a putrescine importer dependent on proton-motive force and is indispensable when Escherichia coli grows on putrescine as a sole carbon or nitrogen source. PlaP is a proton-dependent putrescine importer that is important when Escherichia coli exhibits surface motility. PotE is responsible for both excretion and uptake of putrescine. PotE is a proton-dependent putrescine importer at neutral pH, but at acidic pH PotE is a putrescine-ornithine antiporter |
-, 751075 |
| 7.6.2.11 | more |
ABC uptake transporters typically comprise one periplasmic solute-binding protein (SBP), two integral membrane proteins (transmembrane domains [TMD]) and two nucleotide-binding domains (NBD) that hydrolyze ATP in the cytoplasm, in which the TMD and NBD may be homo- or heterodimers |
-, 751585 |
| 7.6.2.11 | more |
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 |
-, 751493 |
| 7.6.2.11 | physiological function |
the natural function of the SapBCDF enzyme complex is the export of putrescine, Escherichia coli can grow on putrescine as a sole carbon or nitrogen source |
-, 751075 |
| 7.6.2.11 | 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 |
-, 751493 |
