AC   MF_01183;
DC   Protein; auto
TR   HAMAP; MF_01183; -; 1; level=0
XX
Names: Chaperone_SurA
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ID   SURA
DE   RecName: Full=Chaperone SurA;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase SurA;
DE            Short=PPIase SurA;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase SurA;
DE   Flags: Precursor;
GN   Name=surA;
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CC   -!- FUNCTION: Chaperone involved in the correct folding and assembly of
CC       outer membrane proteins. Recognizes specific patterns of aromatic
CC       residues and the orientation of their side chains, which are found more
CC       frequently in integral outer membrane proteins. May act in both early
CC       periplasmic and late outer membrane-associated steps of protein
CC       maturation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Periplasm. Note=Is capable of associating with
CC       the outer membrane.
CC   -!- DOMAIN: The PPIase activity resides only in the second parvulin domain.
CC       The N-terminal region and the C-terminal tail are necessary and
CC       sufficient for the chaperone activity of SurA. The PPIase activity is
CC       dispensable for SurA to function as a chaperone. The N-terminal region
CC       and the C-terminal tail are also required for porin recognition.
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DR   PROSITE; PS01096; PPIC_PPIASE_1; 2; trigger=no
DR   PROSITE; PS50198; PPIC_PPIASE_2; 2; trigger=yes
DR   Pfam; PF00639; Rotamase; 2; trigger=no
DR   General; Signal; -; 1; trigger=yes
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KW   Chaperone
KW   Isomerase
KW   Periplasm
KW   Repeat
KW   Rotamase
KW   Signal
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GO   GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity
GO   GO:0051082; F:unfolded protein binding
GO   GO:0006457; P:protein folding
GO   GO:0042597; C:periplasmic space
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FT   None
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Size: 417-519;
Related: None;
Template: P0ABZ6;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.18 2023/01/26
//