Protein Family Models

This domain is found at the N-terminus of the chaperone SurA and related proteins such as PpiD and foldase PrsA [1,2]. It is a helical domain that together with the C-terminal, forms a domain containing substrate-binding sites [2,3]. The C-terminal of the SurA protein folds back and forms part of this domain also but is not included in the current alignment. [1]. 12429090. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Bitto E, McKay DB;. Structure. 2002;10:1489-1498. [2]. 20970503. The crystal structure of the leptospiral hypothetical protein LIC12922 reveals homology with the periplasmic chaperone SurA. Giuseppe PO, Von Atzingen M, Nascimento AL, Zanchin NI, Guimaraes BG;. J Struct Biol. 2011;173:312-322. [3]. 32358557. Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients. Calabrese AN, Schiffrin B, Watson M, Karamanos TK, Walko M, Humes JR, Horne JE, White P, Wilson AJ, Kalli AC, Tuma R, Ashcroft AE, Brockwell DJ, Radford SE;. Nat Commun. 2020;11:2155. (from Pfam)

Date:

2024-10-16

This domain is found at the N-terminal of the chaperone SurA and related proteins such as PpiD and foldase PrsA [1,2,3]. This is a helical domain that together with the C-terminal forms a domain containing substrate-binding sites [2,3]. The C-terminal of the SurA protein folds back and forms part of this domain also but is not included in the current alignment. [1]. 12429090. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Bitto E, McKay DB;. Structure. 2002;10:1489-1498. [2]. 32358557. Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients. Calabrese AN, Schiffrin B, Watson M, Karamanos TK, Walko M, Humes JR, Horne JE, White P, Wilson AJ, Kalli AC, Tuma R, Ashcroft AE, Brockwell DJ, Radford SE;. Nat Commun. 2020;11:2155. [3]. 20970503. The crystal structure of the leptospiral hypothetical protein LIC12922 reveals homology with the periplasmic chaperone SurA. Giuseppe PO, Von Atzingen M, Nascimento AL, Zanchin NI, Guimaraes BG;. J Struct Biol. 2011;173:312-322. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline. (from Pfam)

Date:

2024-08-14

This domain is found at the N-terminal of the chaperone SurA, a chaperone that assists correct folding of outer membrane proteins (OMPs) in Gram-negative bacteria [1]. This is the helical domain found at the N-terminal of SurA that, together with the C-terminal, forms a core domain which contains OMP binding sites. OMP binding induces conformational changes of SurA domains that protect OMPs from misfolding and aggregation [2]. The C-terminal of the SurA protein folds back and forms part of this domain also but is not included in the current alignment. [1]. 12429090. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Bitto E, McKay DB;. Structure. 2002;10:1489-1498. [2]. 32358557. Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients. Calabrese AN, Schiffrin B, Watson M, Karamanos TK, Walko M, Humes JR, Horne JE, White P, Wilson AJ, Kalli AC, Tuma R, Ashcroft AE, Brockwell DJ, Radford SE;. Nat Commun. 2020;11:2155. (from Pfam)

Date:

2024-10-16

Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline. (from Pfam)

Date:

2024-08-14

peptidylprolyl isomerase SurA protein is a periplasmic molecular chaperone that facilitates correct folding of outer membrane porins, catalyzing the interconversion of cis- and trans-peptidylproline

Date:

2018-03-22

Gene:

surA

Date:

2021-09-01