U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 7

1.

thioredoxin fold domain-containing protein

Date:
2024-08-14
Family Accession:
NF024498.5
Method:
HMM
2.

disulfide isomerase DsbC N-terminal domain-containing protein

This is the N-terminal domain of the disulfide bond isomerase DsbC. The whole molecule is V-shaped, where each arm is a DsbC monomer of two domains linked by a hinge; and the N-termini of each monomer join to form the dimer interface at the base of the V, so are vital for dimerisation [1]. DsbC is required for disulfide bond formation and functions as a disulfide bond isomerase during oxidative protein-folding in bacterial periplasm. It also has chaperone activity [2]. [1]. 10700276. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P;. Nat Struct Biol. 2000;7:196-199. [2]. 16087673. Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. Hiniker A, Collet JF, Bardwell JC;. J Biol Chem. 2005;280:33785-33791. (from Pfam)

Date:
2024-10-16
Family Accession:
NF021896.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

DsbC family protein

DsbC family protein such as the DsbC/DsbG homolog DsbP, which is a novel domain-swapped dimeric protein-disulfide isomerase encoded by the multidrug resistance IncA/C transferable plasmid and is associated with conjugation

Date:
2024-05-10
Family Accession:
10122483
Method:
Sparcle
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center