Pay an invoice 
Site dsbB
- Name: dsbB
- Type: Gene
- Synonyms
b1185 MG1655 locus tag iarB increase ampicillin resistance, by Alksne et al. - Mnemonic: disulfide bond
- Left End Point: 26.55
- Right End Point: 26.56
- Products:
a protein disulfide isomerase (PDI), or PDI-like protein disulfide oxidoreductase - Direction: <
- Priority: 0
- 2 Alleles of This Gene
dsbB2::kan dsbB774(del)::kan - External Database Links:
Host Site Page Links EcoGene.org EG11393 EcoliWiki dsbB - Comment:
- DTT-sensitive phenotype. PPI's act in periplasm and are located in periplasm or inner membrane with active site facing periplasm. Reoxidizes DsbA after its disulfide donations to peripl.proteins.
- References:
- Missiakas, D., C. Georgopoulos, S. Raina 1993. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Proc.Natl.Acad.Sci.USA 90:7084-7088
- Belin, P., P.L. Boquet 1993. [A second gene involved in the formation of disulfide bonds in proteins localized in Escherichia coli periplasmic space]. C.R.Acad.Sci.Ser.III 316:469-473
- Bardwell, J.C., J.O. Lee, G. Jander, N. Martin, D. Belin, J.R. Beckwith 1993. A pathway for disulfide bond formation in vivo. Proc.Natl.Acad.Sci.USA 90:1038-1042
- Jander, G., N.L. Martin, J.R. Beckwith 1994. Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. EMBO J. 13:5121-5127
- Kishigami, S., E. Kanaya, M. Kikuchi, K. Ito 1995. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. J.Biol.Chem. 270:17072-17074
- Guilhot, C., G. Jander, N.L. Martin, J.R. Beckwith 1995. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc.Natl.Acad.Sci.USA 92:9895-9899
- Alksne, L.E., D. Keeney, B.A. Rasmussen 1995. A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, Cc
- Sambongi, Y., S.J. Ferguson 1996. Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds. FEBS Lett. 398:265-268
- Bader, M., W. Muse, T. Zander, J. Bardwell 1998. Reconstitution of a protein disulfide catalytic system. J.Biol.Chem. 273:10302-10307