Editing PEP group translocation (section)

{{short description|Bacterial metabolic pathway}}
'''PEP (phosphoenol pyruvate) group translocation''', also known as the '''phosphotransferase system''' or '''PTS''', is a distinct method used by [[bacteria]] for sugar uptake where the source of energy is from [[phosphoenolpyruvate]] (PEP). It is known to be a multicomponent system that always involves enzymes of the [[plasma membrane]] and those in the [[cytoplasm]].

The PTS system uses active transport. After the translocation across the membrane, the metabolites transported are modified. The PTS system was discovered by [[Saul Roseman]] in 1964.<ref>{{cite journal | vauthors = Bramley HF, Kornberg HL | title = Sequence homologies between proteins of bacterial phosphoenolpyruvate-dependent sugar phosphotransferase systems: identification of possible phosphate-carrying histidine residues | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 14 | pages = 4777–80 | date = July 1987 | pmid = 3299373 | pmc = 305188 | doi = 10.1073/pnas.84.14.4777 | bibcode = 1987PNAS...84.4777B | doi-access = free }}</ref> The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) transports and phosphorylates its sugar substrates in a single energy-coupled step. This transport process is dependent on several cytoplasmic phosphoryl transfer proteins - Enzyme I (I), HPr, Enzyme IIA (IIA), and Enzyme IIB (IIB)) as well as the integral membrane sugar permease (IIC).The PTS Enzyme II complexes are derived from independently evolving 4 PTS Enzyme II complex superfamilies, that include the (1) [[PTS-GFL superfamily|Glucose (Glc)]], (2) [[PTS Mannose-Fructose-Sorbose Family|Mannose (Man)]],<ref>{{Cite journal|last1=Liu|first1=Xueli|last2=Zeng|first2=Jianwei|last3=Huang|first3=Kai|last4=Wang|first4=Jiawei|date=2019-06-17|title=Structure of the mannose transporter of the bacterial phosphotransferase system|journal=Cell Research|doi=10.1038/s41422-019-0194-z|issn=1748-7838|pmid=31209249|pmc=6796895|volume=29|issue=8|pages=680–682}}</ref><ref>{{Cite journal|last1=Huang|first1=Kai|last2=Zeng|first2=Jianwei|last3=Liu|first3=Xueli|last4=Jiang|first4=Tianyu|last5=Wang|first5=Jiawei|date=2021-04-06|title=Structure of the mannose phosphotransferase system (man-PTS) complexed with microcin E492, a pore-forming bacteriocin|journal=Cell Discovery|volume=7|issue=1|pages=20|doi=10.1038/s41421-021-00253-6|issn=2056-5968|pmc=8021565|pmid=33820910}}</ref> (3) [[Permease of phosphotransferase system|Ascorbate-Galactitol (Asc-Gat)]]<ref>{{cite journal | vauthors = Luo P, Yu X, Wang W, Fan S, Li X, Wang J | title = Crystal structure of a phosphorylation-coupled vitamin C transporter | journal = Nature Structural & Molecular Biology | volume = 22 | issue = 3 | pages = 238–41 | date = March 2015 | pmid = 25686089 | doi = 10.1038/nsmb.2975 | s2cid = 9955621 }}</ref><ref>{{cite journal | vauthors = Luo P, Dai S, Zeng J, Duan J, Shi H, Wang J | title = Inward-facing conformation of l-ascorbate transporter suggests an elevator mechanism | journal = Cell Discovery | volume = 4 | pages = 35 | date = 2018 | pmid = 30038796 | pmc = 6048161 | doi = 10.1038/s41421-018-0037-y }}</ref> and (4) Dihydroxyacetone (DHA) superfamilies.<ref>{{cite journal|vauthors=Saier MH|title=The Bacterial Phosphotransferase System: New frontiers 50 years after its discovery|journal=Journal of Molecular Microbiology and Biotechnology|volume=25|issue=2-3|pages=73-78|year=2015|pmid=26159069|pmc=4512285|doi=10.1159/000381215|doi-access=free}}</ref><ref>{{cite journal|vauthors=Bächler C, Schneider P, Bähler P, Lustig A, Erni B|title=Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR|journal=The EMBO Journal|volume=24|issue=2|pages=283-293|pmid=15616579|year=2005|pmc=545809|doi=10.1038/sj.emboj.7600517|doi-access=free}}</ref>