SURA

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 function as a SurA protein with a deletion of the parvulin domains is almost completely functional in vivo. The N-terminal region and the C-terminal tail are also required for porin recognition.

Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB (PubMed:8985185). Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins (PubMed:8985185). May act in both early periplasmic and late outer membrane-associated steps of protein maturation (PubMed:2165476). Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis (PubMed:16267292).

• Periplasm
• Is capable of associating with the outer membrane.

b0053, JW0052, surA, Chaperone SurA, Peptidyl-prolyl cis-trans isomerase SurA, Rotamase SurA, Survival protein A, PPIase SurA

• swissprot:P0ABZ6

Proteins

47284Da