Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Combined Automated Annotation using Multiple IEA Methods
The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.
-
SurA has PPIase-independent chaperone activity mediated by N-terminal and C-terminal domains
-
SurA preferentially binds porins with >50-fold selectivity
-
PPIase domains are dispensable for in vivo function
Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth.
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
-
SurA is the primary chaperone for periplasmic transit of OMPs to the BAM complex
-
SurA interacts directly with BamA/YaeT in vivo
-
SurA depletion causes marked decrease in outer membrane density
-
Skp/DegP serve as a rescue pathway when SurA is absent
Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry.
The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli.
-
FimD levels dramatically reduced (~30-fold) in surA null mutant
-
FimD has higher dependency on SurA than other OMPs
-
SurA-BamB pathway is the primary route for FimD assembly
Genetic, biochemical, and molecular characterization of the polypeptide transport-associated domain of Escherichia coli BamA.
Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains.
Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins.
-
SurA characterized as a holdase chaperone
-
SurA stabilizes dynamic unfolded state of FhuA
-
SurA-chaperoned FhuA inserts beta-hairpins stepwise into the membrane
-
Membrane acts as free-energy sink for beta-hairpin insertion
SurA assists the folding of Escherichia coli outer membrane proteins.
-
SurA required for efficient folding of OmpA, OmpF, and LamB in vivo
-
Folding of periplasmic proteins is independent of SurA
-
Trypsin sensitivity used as folding assay
SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins.
-
SurA has PPIase activity and participates in LamB assembly
-
SurA required for conversion of unfolded monomers to folded monomers
-
Absence of SurA blocks assembly pathway
-
Loss of SurA induces sigmaE stress response
The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins.
The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition.
Current PAINT annotations for PANTHER family PTHR47637
-
PTN005352065 currently carries IBD assertions for protein folding, PPIase activity, and periplasmic localization, each seeded by P0ABZ6; it no longer carries GO:0051082.
Unfolded Protein Binding Annotation Review
Deep research synthesis for E. coli SurA