HAMAP

Accession	MF_01183
Dates	1-DEC-2006 (Created) 2-DEC-2011 (Last updated, Version 11)

Data class

Protein

Predictors

HAMAP; MF_01183; [distribution of match scores in UniProtKB];[seed alignment for MF_01183]

Names

Chaperone_SurA

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. It 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 (By similarity).

CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0).

SUBCELLULAR LOCATION: Periplasm (By similarity). Note=Is capable of associating with the outer membrane (By similarity).

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 (By similarity).

SIMILARITY: Contains 2 PpiC domains.

PROSITE	PS01096; PPIC_PPIASE_1; 2; PS50198; PPIC_PPIASE_2; 2; trigger=PRU00278;
Pfam	PF00639; Rotamase; 2;
General	Signal; -; 1; trigger=Yes;

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.

Size range:	417-519 amino acids
Related UniRules:	None
Template:	P0ABZ6 (SURA_ECOLI)
Scope:	Bacteria; Proteobacteria
Fusion:	Nter: None; Cter: None
Duplicate:	None
Plasmid encoded:	None