P76352
Gene name |
yeeO (b1985, JW1965) |
Protein name |
Probable FMN/FAD exporter YeeO |
Names |
|
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b1985 |
EC number |
|
Protein Class |
|

Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

1 structures for P76352
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-P76352-F1 | Predicted | AlphaFoldDB |
No variants for P76352
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for P76352 |
No associated diseases with P76352
No regional properties for P76352
Type | Name | Position | InterPro Accession |
---|---|---|---|
No domain, repeats, and functional sites for P76352 |
3 GO annotations of cellular component
Name | Definition |
---|---|
integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 GO annotations of molecular function
Name | Definition |
---|---|
antiporter activity | Enables the active transport of a solute across a membrane by a mechanism whereby two or more species are transported in opposite directions in a tightly coupled process not directly linked to a form of energy other than chemiosmotic energy. The reaction is: solute A(out) + solute B(in) = solute A(in) + solute B(out). |
dipeptide transmembrane transporter activity | Enables the transfer of a dipeptide from one side of a membrane to the other. A dipeptide is a combination of two amino acids linked together by a peptide (-CO-NH-) bond. |
FAD transmembrane transporter activity | Enables the directed movement of flavin-adenine dinucleotide (FAD) from one side of a membrane to the other. FAD forms the coenzyme of the prosthetic group of various flavoprotein oxidoreductase enzymes, in which it functions as an electron acceptor by being reversibly converted to its reduced form. |
FMN transmembrane transporter activity | Enables the directed movement of flavine mononucleotide (FMN) from one side of a membrane to the other. |
xenobiotic transmembrane transporter activity | Enables the directed movement of a xenobiotic from one side of a membrane to the other. A xenobiotic is a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. |
3 GO annotations of biological process
Name | Definition |
---|---|
dipeptide transmembrane transport | The directed movement of a dipeptide across a membrane by means of some agent such as a transporter or pore. A dipeptide is a combination of two amino acids linked together by a peptide (-CO-NH-) bond. |
FAD transmembrane transport | The process in which flavin-adenine dinucleotide (FAD) is transported across a membrane. FAD forms the coenzyme of the prosthetic group of various flavoprotein oxidoreductase enzymes, in which it functions as an electron acceptor by being reversibly converted to its reduced form. |
protein transport | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
No homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
No homologous proteins |
10 | 20 | 30 | 40 | 50 | 60 |
MLRHILTAKN | LLSNPIFKFP | NCLPFLSTVC | CICRQFVGEN | LCSFADSPSL | FEMWFHFLQL |
70 | 80 | 90 | 100 | 110 | 120 |
RSALNISSAL | RQVVHGTRWH | AKRKSYKVLF | WREITPLAVP | IFMENACVLL | MGVLSTFLVS |
130 | 140 | 150 | 160 | 170 | 180 |
WLGKDAMAGV | GLADSFNMVI | MAFFAAIDLG | TTVVVAFSLG | KRDRRRARVA | TRQSLVIMTL |
190 | 200 | 210 | 220 | 230 | 240 |
FAVLLATLIH | HFGEQIIDFV | AGDATTEVKA | LALTYLELTV | LSYPAAAITL | IGSGALRGAG |
250 | 260 | 270 | 280 | 290 | 300 |
NTKIPLLING | SLNILNIIIS | GILIYGLFSW | PGLGFVGAGL | GLTISRYIGA | VAILWVLAIG |
310 | 320 | 330 | 340 | 350 | 360 |
FNPALRISLK | SYFKPLNFSI | IWEVMGIGIP | ASVESVLFTS | GRLLTQMFVA | GMGTSVIAGN |
370 | 380 | 390 | 400 | 410 | 420 |
FIAFSIAALI | NLPGSALGSA | STIITGRRLG | VGQIAQAEIQ | LRHVFWLSTL | GLTAIAWLTA |
430 | 440 | 450 | 460 | 470 | 480 |
PFAGVMASFY | TQDPQVKHVV | VILIWLNALF | MPIWSASWVL | PAGFKGARDA | RYAMWVSMLS |
490 | 500 | 510 | 520 | 530 | 540 |
MWGCRVVVGY | VLGIMLGWGV | VGVWMGMFAD | WAVRAVLFYW | RMVTGRWLWK | YPRPEPQKCE |
KKPVVSE |