Q5PDE6 · SURA_SALPA
- ProteinChaperone SurA
- GenesurA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids428 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | outer membrane-bounded periplasmic space | |
Molecular Function | peptide binding | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Molecular Function | unfolded protein binding | |
Biological Process | Gram-negative-bacterium-type cell outer membrane assembly | |
Biological Process | protein folding | |
Biological Process | protein stabilization |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameChaperone SurA
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionQ5PDE6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Is capable of associating with the outer membrane.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-20 | ||||
Chain | PRO_0000270035 | 21-428 | Chaperone SurA | ||
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 171-272 | PpiC 1 | |||
Domain | 282-382 | PpiC 2 | |||
Domain
The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length428
- Mass (Da)47,251
- Last updated2005-01-04 v1
- ChecksumE85BA3468C81E3C8
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000026 EMBL· GenBank· DDBJ | AAV76126.1 EMBL· GenBank· DDBJ | Genomic DNA |