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 Q47258
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3ZUA | NMR | - | A | 2-137 | PDB |
| AF-Q47258-F1 | Predicted | AlphaFoldDB |
No variants for Q47258
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q47258 | |||||
No associated diseases with Q47258
6 regional properties for Q47258
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ABC transporter-like, ATP-binding domain | 468 - 703 | IPR003439 |
| domain | AAA+ ATPase domain | 494 - 680 | IPR003593 |
| domain | Peptidase C39, bacteriocin processing | 3 - 129 | IPR005074 |
| domain | ABC transporter type 1, transmembrane domain | 157 - 436 | IPR011527 |
| conserved_site | ABC transporter-like, conserved site | 606 - 620 | IPR017871 |
| domain | Peptidase C39-like A | 3 - 125 | IPR039395 |
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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| type I protein secretion system complex | A complex of three secretory proteins that carry out secretion in the type I secretion system: an inner membrane transport ATPase (termed ABC protein for ATP-binding cassette), which provides the energy for protein secretion; an outer membrane protein, which is exported via the sec pathway; and a membrane fusion protein, which is anchored in the inner membrane and spans the periplasmic space. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ABC-type transporter activity | Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| peptidase activity | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein secretion by the type I secretion system | The process in which proteins are secreted into the extracellular milieu via the type I secretion system; secretion occurs in a continuous process without the distinct presence of periplasmic intermediates and does not involve proteolytic processing of secreted proteins. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDSCHKIDYG | LYALEILAQY | HNVSVNPEEI | KHRFDTDGTG | LGLTSWLLAA | KSLELKVKQV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KKTIDRLNFI | SLPALVWRED | GRHFILTKVS | KEANRYLIFD | LEQRNPRVLE | QSEFEALYQG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HIILIASRSS | VAGKLAKFDF | TWFIPAIIKY | RRIFIETLVV | SVFLQLFALI | TPLFFQVVMD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KVLVHRGFST | LNVITVALSV | VVVFEIILSG | LRTYIFAHST | SRIDVELGAK | LFRHLLALPI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SYFESRRVGD | TVARVRELDQ | IRNFLTGQAL | TSVLDLLFSF | IFFAVMWYYS | PKLTLVILFS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LPCYAAWSVF | ISPILRRRLD | DKFSRNADNQ | SFLVESVTAI | NTIKAMAVSP | QMTNIWDKQL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AGYVAAGFKV | TVLATIGQQG | IQLIQKTVMI | INLWLGAHLV | ISGDLSIGQL | IAFNMLAGQI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VAPVIRLAQI | WQDFQQVGIS | VTRLGDVLNS | PTESYHGKLA | LPEINGDITF | RNIRFRYKPD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SPVILDNINL | SIKQGEVIGI | VGRSGSGKST | LTKLIQRFYI | PENGQVLIDG | HDLALADPNW |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LRRQVGVVLQ | DNVLLNRSII | DNISLANPGM | SVEKVIYAAK | LAGAHDFISE | LREGYNTIVG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EQGAGLSGGQ | RQRIAIARAL | VNNPKILIFD | EATSALDYES | EHIIMRNMHK | ICKGRTVIII |
| 670 | 680 | 690 | 700 | ||
| AHRLSTVKNA | DRIIVMEKGK | IVEQGKHKEL | LSEPESLYSY | LYQLQSD |