P38054
Gene name |
cusA (ybdE, b0575, JW0564) |
Protein name |
Cation efflux system protein CusA |
Names |
|
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b0575 |
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
16 structures for P38054
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3K07 | X-ray | 352 A | A | 1-1047 | PDB |
| 3K0I | X-ray | 412 A | A | 1-1047 | PDB |
| 3KSO | X-ray | 437 A | A | 1-1047 | PDB |
| 3KSS | X-ray | 388 A | A | 1-1047 | PDB |
| 3NE5 | X-ray | 290 A | A | 2-1047 | PDB |
| 3T51 | X-ray | 390 A | A | 1-1047 | PDB |
| 3T53 | X-ray | 337 A | A | 1-1047 | PDB |
| 3T56 | X-ray | 342 A | A | 1-1047 | PDB |
| 4DNR | X-ray | 368 A | A | 1-1047 | PDB |
| 4DNT | X-ray | 310 A | A | 1-1047 | PDB |
| 4DOP | X-ray | 420 A | A | 1-1047 | PDB |
| 7KF5 | EM | 320 A | A/B/C | 1-1047 | PDB |
| 7KF6 | EM | 340 A | A/B/C | 1-1047 | PDB |
| 7KF7 | EM | 280 A | A/B/C | 1-1047 | PDB |
| 7KF8 | EM | 300 A | A/B/C | 1-1047 | PDB |
| AF-P38054-F1 | Predicted | AlphaFoldDB |
No variants for P38054
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P38054 | |||||
No associated diseases with P38054
No regional properties for P38054
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P38054 | |||
2 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| silver ion transmembrane transporter activity | Enables the transfer of silver (Ag) ions 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. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| copper ion export | The directed movement of copper ions out of a cell or organelle. |
| copper ion transmembrane transport | The directed movement of copper cation across a membrane. |
| response to copper ion | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a copper ion stimulus. |
| response to silver ion | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a silver ion stimulus. |
| response to toxic substance | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a toxic stimulus. |
| silver ion transmembrane transport | The directed movement of silver ion across a membrane. |
| silver ion transport | The directed movement of silver (Ag) ions 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 |
| MIEWIIRRSV | ANRFLVLMGA | LFLSIWGTWT | IINTPVDALP | DLSDVQVIIK | TSYPGQAPQI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VENQVTYPLT | TTMLSVPGAK | TVRGFSQFGD | SYVYVIFEDG | TDPYWARSRV | LEYLNQVQGK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LPAGVSAELG | PDATGVGWIY | EYALVDRSGK | HDLADLRSLQ | DWFLKYELKT | IPDVAEVASV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GGVVKEYQVV | IDPQRLAQYG | ISLAEVKSAL | DASNQEAGGS | SIELAEAEYM | VRASGYLQTL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DDFNHIVLKA | SENGVPVYLR | DVAKVQIGPE | MRRGIAELNG | EGEVAGGVVI | LRSGKNAREV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IAAVKDKLET | LKSSLPEGVE | IVTTYDRSQL | IDRAIDNLSG | KLLEEFIVVA | VVCALFLWHV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RSALVAIISL | PLGLCIAFIV | MHFQGLNANI | MSLGGIAIAV | GAMVDAAIVM | IENAHKRLEE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| WQHQHPDATL | DNKTRWQVIT | DASVEVGPAL | FISLLIITLS | FIPIFTLEGQ | EGRLFGPLAF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TKTYAMAGAA | LLAIVVIPIL | MGYWIRGKIP | PESSNPLNRF | LIRVYHPLLL | KVLHWPKTTL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LVAALSVLTV | LWPLNKVGGE | FLPQINEGDL | LYMPSTLPGI | SAAEAASMLQ | KTDKLIMSVP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EVARVFGKTG | KAETATDSAP | LEMVETTIQL | KPQEQWRPGM | TMDKIIEELD | NTVRLPGLAN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LWVPPIRNRI | DMLSTGIKSP | IGIKVSGTVL | ADIDAMAEQI | EEVARTVPGV | ASALAERLEG |
| 730 | 740 | 750 | 760 | 770 | 780 |
| GRYINVEINR | EKAARYGMTV | ADVQLFVTSA | VGGAMVGETV | EGIARYPINL | RYPQSWRDSP |
| 790 | 800 | 810 | 820 | 830 | 840 |
| QALRQLPILT | PMKQQITLAD | VADIKVSTGP | SMLKTENARP | TSWIYIDARD | RDMVSVVHDL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| QKAIAEKVQL | KPGTSVAFSG | QFELLERANH | KLKLMVPMTL | MIIFVLLYLA | FRRVGEALLI |
| 910 | 920 | 930 | 940 | 950 | 960 |
| ISSVPFALVG | GIWLLWWMGF | HLSVATGTGF | IALAGVAAEF | GVVMLMYLRH | AIEAVPSLNN |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| PQTFSEQKLD | EALYHGAVLR | VRPKAMTVAV | IIAGLLPILW | GTGAGSEVMS | RIAAPMIGGM |
| 1030 | 1040 | ||||
| ITAPLLSLFI | IPAAYKLMWL | HRHRVRK |