Q8DED4
Gene name |
surA |
Protein name |
Chaperone SurA |
Names |
Peptidyl-prolyl cis-trans isomerase SurA, PPIase SurA, Rotamase SurA |
Species |
Vibrio vulnificus (strain CMCP6) |
KEGG Pathway |
vvu:VV1_0661 |
EC number |
5.2.1.8: Cis-trans isomerases |
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 Q8DED4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8DED4-F1 | Predicted | AlphaFoldDB |
No variants for Q8DED4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8DED4 | |||||
No associated diseases with Q8DED4
4 regional properties for Q8DED4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Zinc finger, CCCH-type | 88 - 122 | IPR000571-1 |
| domain | Zinc finger, CCCH-type | 134 - 164 | IPR000571-2 |
| conserved_site | tRNA-dihydrouridine synthase, conserved site | 378 - 396 | IPR018517 |
| domain | DUS-like, FMN-binding domain | 292 - 572 | IPR035587 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.2.1.8 | Cis-trans isomerases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| outer membrane-bounded periplasmic space | The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| peptide binding | Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds. |
| peptidyl-prolyl cis-trans isomerase activity | Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). |
| unfolded protein binding | Binding to an unfolded protein. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| Gram-negative-bacterium-type cell outer membrane assembly | The assembly of an outer membrane of the type formed in Gram-negative bacteria. This membrane is enriched in polysaccharide and protein, and the outer leaflet of the membrane contains specific lipopolysaccharide structures. |
| protein folding | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. |
| protein stabilization | Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNIWKTLLLG | MLVTGSAVSA | PVELDKVAVI | VNDGVILQSD | IDTATKTLRA | NAKKSGQALP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DADVLNEQIV | DKLIIDTLQT | QEADRIGVRI | DDTRLNQAIE | EIARNNNQTI | DELSAAIASE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GVSYAEFREQ | IRKEMAASEA | RNALVRRRIN | ILPAEVDNLA | ELLSKETNAS | VEYRIGHIQL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RFTDGQDKSA | LEAQAKELVE | KLKQGADFST | MAYTYSKGPK | ALQGGDWGWM | RKEEMPTIFA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DQIKMQNKGS | IIGPFRSGVG | FHILKIEDVK | GLETVAVTEV | NARHILLKPT | VILSDEGAQR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ELNEFIRRIR | AGEATFGELA | QQYSQDPGSA | AQDGELGYQT | PDLYVPEFKH | QVETLPVGTI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SEPFKTVHGW | HIVEVLDRRE | VDRTDSAMKN | KAYRILFNRK | FNEEVGAWMQ | ELRAGAFVEI |
| INEEENDG |