HAMAP rule MF_01183

General rule information [?]

Accession	MF_01183
Dates	1-DEC-2006 (Created) 26-JAN-2023 (Last updated, Version 18)
Name	Chaperone_SurA
Scope(s)	Bacteria Pseudomonadota
Template(s)	P0ABZ6 (SURA_ECOLI); [ Recover all ]
Triggered by	HAMAP; MF_01183 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier	SURA
Protein name	RecName: Full=Chaperone SurA; AltName: Full=Peptidyl-prolyl cis-trans isomerase SurA; Short=PPIase SurA; EC=5.2.1.8; AltName: Full=Rotamase SurA; Flags: Precursor;
Gene name	Name=surA;

Comments [?]

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	Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8;
SUBCELLULAR LOCATION	Periplasm. Note=Is capable of associating with the outer membrane.
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 [?]

Gene Ontology [?]

GO:0003755; Molecular function:peptidyl-prolyl cis-trans isomerase activity

GO:0051082; Molecular function:unfolded protein binding

GO:0006457; Biological process:protein folding

GO:0042597; Cellular component:periplasmic space

Cross-references [?]

Features [?]

Additional information [?]