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 P26760
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P26760-F1 | Predicted | AlphaFoldDB |
8 variants for P26760
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 110 | E>KQT | strain: Serotype 5 [UniProt] | No | ||
| 328 | D>H | strain: Serotype 5 [UniProt] | No | ||
| 517 | R>V | strain: Serotype 5 [UniProt] | No | ||
| 556 | N>G | strain: Serotype 5 [UniProt] | No | ||
| 609 | G>RAT | strain: S 4074 / Serotype 1 [UniProt] | No | ||
| 611 | R>PN | strain: Serotype 5 [UniProt] | No | ||
| 671 | D>AS | strain: Serotype 5 [UniProt] | No | ||
| 692 | A>R | strain: Serotype 5 [UniProt] | No |
No associated diseases with P26760
6 regional properties for P26760
| 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 | 5 - 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 | 8 - 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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| hemolysis in another organism | The cytolytic destruction of red blood cells, with the release of intracellular hemoglobin, in one organism by another. |
| 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 |
| MDFYREEDYG | LYALTILAQY | HNIAVNPEEL | KHKFDLEGKG | LDLTAWLLAA | KSLELKAKQV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KKAIDRLAFI | ALPALVWRED | GKHFILTKID | NEAKKYLIFD | LETHNPRILE | QAEFESLYQG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KLILVASRAS | IVGKLAKFDF | TWFIPAVIKY | RKIFIETLIV | SIFLQIFALI | TPLFFQVVMD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KVLVHRGFST | LNVITVALAI | VVLFEIVLNG | LRTYIFAHST | SRIDVELGAR | LFRHLLALPI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SYFENRRVGD | TVARVRELDQ | IRNFLTGQAL | TSVLDLMFSF | IFFAVMWYYS | PKLTLVILGS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LPFYMGWSIF | ISPILRRRLD | EKFARGADNQ | SFLVESVTAI | NTIKALAVTP | QMTNTWDKQL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ASYVSAGFRV | TTLATIGQQG | VQFIQKVVMV | ITLWLGAHLV | ISGDLSIGQL | IAFNMLSGQV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IAPVIRLAQL | WQDFQQVGIS | VTRLGDVLNS | PTESYQGKLA | LPEIKGDITF | RNIRFRYKPD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| APVILNDVNL | SIQQGEVIGI | VGRSGSGKST | LTKLIQRFYI | PENGQVLIDG | HDLALADPNW |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LRRQVGVVLQ | DNVLLNRSIR | DNIALADPGM | PMEKIVHAAK | LAGAHEFISE | LREGYNTIVG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EQGAGLSGGQ | RQRIAIARAL | VNNPKILIFD | EATSALDYES | EHIIMRNMHQ | ICKGRTVIII |
| 670 | 680 | 690 | 700 | ||
| AHRLSTVKNA | DRIIVMEKGQ | IVEQGKHKEL | LADPNGLYHY | LHQLQSE |