P06972
Gene name |
fhuB (b0153, JW0149) |
Protein name |
Iron(3+)-hydroxamate import system permease protein FhuB |
Names |
Ferric hydroxamate uptake protein B, Ferrichrome transport system permease protein FhuB, Ferrichrome uptake protein FhuB, Iron(III)-hydroxamate import system permease protein FhuB |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b0153 |
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
2 structures for P06972
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 7LB8 | EM | 340 A | B | 1-660 | PDB |
| AF-P06972-F1 | Predicted | AlphaFoldDB |
No variants for P06972
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P06972 | |||||
No associated diseases with P06972
No regional properties for P06972
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P06972 | |||
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| ATP-binding cassette (ABC) transporter complex | A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter. |
| ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing | A complex for the transport of metabolites into the cell, consisting of 5 subunits: two ATP-binding subunits, two membrane spanning subunits, and one substrate-binding subunit. In organisms with two membranes, the substrate-binding protein moves freely in the periplasmic space and joins the other subunits only when bound with substrate. In organisms with only one membrane the substrate-binding protein is tethered to the cytoplasmic membrane and associated with the other subunits. Transport of the substrate across the membrane is driven by the hydrolysis of ATP. |
| integral component of plasma membrane | The component of the plasma 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. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| transmembrane transporter activity | Enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| iron ion import across plasma membrane | The directed movement of iron ions from outside of a cell, across the plasma membrane and into the cytosol. |
| siderophore-dependent iron import into cell | A process in which iron (Fe3+) is solubilized by ferric iron-specific chelators, known as siderophores, excreted by a cell; the iron-siderophore complex is then transported into the cell by specific cell surface receptors. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSKRIALFPA | LLLALLVIVA | TALTWMNFSQ | ALPRSQWAQA | AWSPDIDVIE | QMIFHYSLLP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RLAISLLVGA | GLGLVGVLFQ | QVLRNPLAEP | TTLGVATGAQ | LGITVTTLWA | IPGAMASQFA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AQAGACVVGL | IVFGVAWGKR | LSPVTLILAG | LVVSLYCGAI | NQLLVIFHHD | QLQSMFLWST |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GTLTQTDWGG | VERLWPQLLG | GVMLTLLLLR | PLTLMGLDDG | VARNLGLALS | LARLAALSLA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IVISALLVNA | VGIIGFIGLF | APLLAKMLGA | RRLLPRLMLA | SLIGALILWL | SDQIILWLTR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VWMEVSTGSV | TALIGAPLLL | WLLPRLRSIS | APDMKVNDRV | AAERQHVLAF | ALAGGVLLLM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AVVVALSFGR | DAHGWTWASG | ALLEDLMPWR | WPRIMAALFA | GVMLAVAGCI | IQRLTGNPMA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SPEVLGISSG | AAFGVVLMLF | LVPGNAFGWL | LPAGSLGAAV | TLLIIMIAAG | RGGFSPHRML |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LAGMALSTAF | TMLLMMLQAS | GDPRMAQVLT | WISGSTYNAT | DAQVWRTGIV | MVILLAITPL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| CRRWLTILPL | GGDTARAVGM | ALTPTRIALL | LLAACLTATA | TMTIGPLSFV | GLMAPHIARM |
| 610 | 620 | 630 | 640 | 650 | |
| MGFRRTMPHI | VISALVGGLL | LVFADWCGRM | VLFPFQIPAG | LLSTFIGAPY | FIYLLRKQSR |