HAMAP rule MF_01183

Accession	MF_01183
Dates	1-DEC-2006 (Created) 26-JAN-2023 (Last updated, Version 18)

Name	Chaperone_SurA

Scope

Bacteria; Pseudomonadota

Template

P0ABZ6 (SURA_ECOLI)

Triggered by

HAMAP; MF_01183 (Get profile general information and statistics)

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

surA

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	RHEA:16237: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) 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.

Chaperone
Isomerase
Periplasm
Repeat
Rotamase
Signal

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.

PROSITE	PS01096; PPIC_PPIASE_1; 2;
	PS50198; PPIC_PPIASE_2; 2; trigger=PRU00278;
Pfam	PF00639; Rotamase; 2;

General

Signal; -; 1; trigger=yes;

Size range	417-519 amino acids
Related rules	None
Fusion	None

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