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13  structures 2169  species 1  interaction 2959  sequences 6  architectures

Family: DsbB (PF02600)

Summary: Disulfide bond formation protein DsbB

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This is the Wikipedia entry entitled "Disulfide bond formation protein B". More...

Disulfide bond formation protein B Edit Wikipedia article

2hi7.gif
Disulfide bond formation protein B (red), complex with DsbA (blue)
Identifiers
Symbol DsbB
Pfam PF02600
InterPro IPR003752
TCDB 5.A.2
OPM superfamily 194
OPM protein 2hi7

Disulfide bond formation protein B (DsbB) is a protein component of the pathway that leads to disulfide bond formation in periplasmic proteins of Escherichia coli and other bacteria.

The DsbB protein oxidizes the periplasmic protein DsbA which in turn oxidizes cysteines in other periplasmic proteins in order to make disulfide bonds.[1] DsbB acts as a redox potential transducer across the cytoplasmic membrane. It is a membrane protein which spans the membrane four times with both the N- and C-termini of the protein are in the cytoplasm. Each of the periplasmic domains of the protein has two essential cysteines. The two cysteines in the first periplasmic domain are in a Cys-X-Y-Cys configuration that is characteristic of the active site of other proteins involved in disulfide bond formation, including DsbA and protein disulfide isomerase.[2]

[edit] References

  1. ^ Lee JO, Beckwith J, Bardwell JC, Jander G, Martin N, Belin D (1993). "A pathway for disulfide bond formation in vivo". Proc. Natl. Acad. Sci. U.S.A. 90 (3): 1038–1042. DOI:10.1073/pnas.90.3.1038. PMC 45806. PMID 8430071. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=45806. 
  2. ^ Beckwith J, Jander G, Martin NL (1994). "Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation". EMBO J. 13 (21): 5121–5127. PMC 395459. PMID 7957076. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=395459. 

This article incorporates text from the public domain Pfam and InterPro IPR003752


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Disulfide bond formation protein DsbB Provide feedback

This family consists of disulfide bond formation protein DsbB from bacteria. The DsbB protein oxidises the periplasmic protein DsbA which in turn oxidises cysteines in other periplasmic proteins in order to make disulfide bonds [1]. DsbB acts as a redox potential transducer across the cytoplasmic membrane and is an integral membrane protein [2]. DsbB posses six cysteines four of which are necessary for it proper function in vivo [1].

Literature references

  1. Jander G, Martin NL, Beckwith J; , EMBO J 1994;13:5121-5127.: Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. PUBMED:7957076 EPMC:7957076

  2. Bardwell JC, Lee JO, Jander G, Martin N, Belin D, Beckwith J; , Proc Natl Acad Sci U S A 1993;90:1038-1042.: A pathway for disulfide bond formation in vivo. PUBMED:8430071 EPMC:8430071


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003752

Disulphide bonds contribute to folding, maturation, stability, and regulation of proteins, in particular those localized out of the cytosol. Oxidation of selected pairs of cysteines to disulphide in vivo requires cellular factors present in the bacterial periplasmic space or in the endoplasmic reticulum of eukaryotic cells [PUBMED:12524212, PUBMED:12415301].

DsbB is a protein component of the pathway that leads to disulphide bond formation in periplasmic proteins of Escherichia coli and other bacteria. The DsbB protein oxidises the periplasmic protein DsbA which in turn oxidises cysteines in other periplasmic proteins in order to make disulphide bonds [PUBMED:8430071]. DsbB acts as a redox potential transducer across the cytoplasmic membrane. It is a membrane protein which spans the membrane four times with both the N- and C-termini of the protein are in the cytoplasm. Each of the periplasmic domains of the protein has two essential cysteines. The two cysteines in the first periplasmic domain are in a Cys-X-Y-Cys configuration that is characteristic of the active site of other proteins involved in disulphide bond formation, including DsbA and protein disulphide isomerase [PUBMED:7957076].

This entry also includes disulphide bond formation protein BdbC from Bacillus subtilis which functionally corresponds to the well-characterised E. coli DsbB [PUBMED:11844773].

Gene Ontology

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Domain organisation

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Alignments

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  Seed
(184)
Full
(2959)
Representative proteomes NCBI
(1795)
Meta
(1819)
RP15
(116)
RP35
(272)
RP55
(395)
RP75
(514)
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  Seed
(184)
Full
(2959)
Representative proteomes NCBI
(1795)
Meta
(1819)
RP15
(116)
RP35
(272)
RP55
(395)
RP75
(514)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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Curation and family details

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Seed source: COG1495
Previous IDs: none
Type: Family
Author: Bashton M, Bateman A
Number in seed: 184
Number in full: 2959
Average length of the domain: 155.50 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 77.26 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.1 22.1
Trusted cut-off 22.9 22.1
Noise cut-off 21.7 21.7
Model length: 156
Family (HMM) version: 11
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Species distribution

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Interactions

There is 1 interaction for this family. More...

DSBA

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DsbB domain has been found. There are 13 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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