Difference between revisions of "ECF transporter"
(→The substrate-specific S components of the ECF transporters) |
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* [[YhfU]]: uptake of biotin | * [[YhfU]]: uptake of biotin | ||
* [[TrpP]]: uptake of tryptophan | * [[TrpP]]: uptake of tryptophan | ||
| − | * [[YuiG]]: unknown specificity | + | * [[YuiG]]: unknown specificity, may also transport biotin |
| + | * [[YpdP]]: queuosine precursor uptake | ||
| + | |||
| + | == The class I ECF transporter for thiamine == | ||
| + | * [[ThiU]]: binding protein | ||
| + | * [[ThiV]]: substrate-specific S component | ||
| + | * [[ThiW]]: ATP-binding protein (corresponds to A1 + A2) | ||
| + | * [[ThiX]]: membrane-spanning T protein | ||
== Important reviews and publications == | == Important reviews and publications == | ||
| − | <pubmed>23584589 , 21135102, 20497229, </pubmed> | + | <pubmed>23584589 , 21135102, 20497229, 18931129 22574898 24362466 27273632</pubmed> |
Latest revision as of 17:42, 26 March 2024
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Contents
ECF transporters are required for the uptake of micronutrients such as cofactors (vitamins), metal ions, or amino acids. The transporters are composed of three general components (membrane spanning T protein und two ATP-hydrolyzing A proteins) and substrate-specific S proteins.
In B. subtilis, there are four known substrates for ECF transporters, riboflavin, thiamine, biotin, and tryptophan.
The general components of the ECF transporters
- ybxA ATP-binding A1 protein (EcfA1)
- ybaE ATP-binding A2 protein (EcfA2)
- ybaF membrane-spanning T protein (EcfT)
The substrate-specific S components of the ECF transporters
- RibU: uptake of riboflavin
- ThiT: uptake of thiamine
- YhfU: uptake of biotin
- TrpP: uptake of tryptophan
- YuiG: unknown specificity, may also transport biotin
- YpdP: queuosine precursor uptake
The class I ECF transporter for thiamine
- ThiU: binding protein
- ThiV: substrate-specific S component
- ThiW: ATP-binding protein (corresponds to A1 + A2)
- ThiX: membrane-spanning T protein
Important reviews and publications
Kaspar P Locher
Mechanistic diversity in ATP-binding cassette (ABC) transporters.
Nat Struct Mol Biol: 2016, 23(6);487-93
[PubMed:27273632]
[WorldCat.org]
[DOI]
(I p)
Dirk J Slotboom
Structural and mechanistic insights into prokaryotic energy-coupling factor transporters.
Nat Rev Microbiol: 2014, 12(2);79-87
[PubMed:24362466]
[WorldCat.org]
[DOI]
(I p)
Ke Xu, Minhua Zhang, Qin Zhao, Fang Yu, Hui Guo, Chengyuan Wang, Fangyuan He, Jianping Ding, Peng Zhang
Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis.
Nature: 2013, 497(7448);268-71
[PubMed:23584589]
[WorldCat.org]
[DOI]
(I p)
Guus B Erkens, Maria Majsnerowska, Josy ter Beek, Dirk Jan Slotboom
Energy coupling factor-type ABC transporters for vitamin uptake in prokaryotes.
Biochemistry: 2012, 51(22);4390-6
[PubMed:22574898]
[WorldCat.org]
[DOI]
(I p)
Josy ter Beek, Ria H Duurkens, Guus B Erkens, Dirk Jan Slotboom
Quaternary structure and functional unit of energy coupling factor (ECF)-type transporters.
J Biol Chem: 2011, 286(7);5471-5
[PubMed:21135102]
[WorldCat.org]
[DOI]
(I p)
Thomas Eitinger, Dmitry A Rodionov, Mathias Grote, Erwin Schneider
Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.
FEMS Microbiol Rev: 2011, 35(1);3-67
[PubMed:20497229]
[WorldCat.org]
[DOI]
(I p)
Dmitry A Rodionov, Peter Hebbeln, Aymerick Eudes, Josy ter Beek, Irina A Rodionova, Guus B Erkens, Dirk J Slotboom, Mikhail S Gelfand, Andrei L Osterman, Andrew D Hanson, Thomas Eitinger
A novel class of modular transporters for vitamins in prokaryotes.
J Bacteriol: 2009, 191(1);42-51
[PubMed:18931129]
[WorldCat.org]
[DOI]
(I p)
