Disulfide bond formation protein B
Details
- Name
- Disulfide bond formation protein B
- Synonyms
- Disulfide oxidoreductase
- roxB
- ycgA
- Gene Name
- dsbB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0008312|Disulfide bond formation protein B MLRFLNQCSQGRGAWLLMAFTALALELTALWFQHVMLLKPCVLCIYERCALFGVLGAALI GAIAPKTPLRYVAMVIWLYSAFRGVQLTYEHTMLQLYPSPFATCDFMVRFPEWLPLDKWV PQVFVASGDCAERQWDFLGLEMPQWLLGIFIAYLIVAVLVVISQPFKAKKRDLFGR
- Number of residues
- 176
- Molecular Weight
- 20141.985
- Theoretical pI
- 8.59
- GO Classification
- Functionselectron carrier activity / protein disulfide oxidoreductase activityProcesseselectron transport chain / response to heatComponentsintegral component of membrane / plasma membrane
- General Function
- Protein disulfide oxidoreductase activity
- Specific Function
- Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway.
- Pfam Domain Function
- DsbB (PF02600)
- Transmembrane Regions
- 15-31 50-65 72-89 145-163
- Cellular Location
- Cell inner membrane
- Gene sequence
>lcl|BSEQ0020765|Disulfide bond formation protein B (dsbB) ATGTTGCGATTTTTGAACCAATGTTCACAAGGCCGGGGCGCGTGGCTGTTGATGGCGTTT ACTGCTCTGGCACTGGAACTGACGGCGCTGTGGTTCCAGCATGTGATGTTACTGAAACCT TGCGTGCTCTGTATTTATGAACGCTGCGCGTTATTCGGCGTTCTGGGTGCTGCGCTGATT GGCGCGATCGCCCCGAAAACTCCGCTGCGTTATGTAGCGATGGTTATCTGGTTGTATAGT GCGTTCCGCGGTGTGCAGTTAACTTACGAGCACACCATGCTTCAGCTCTATCCTTCGCCG TTTGCCACCTGTGATTTTATGGTTCGTTTCCCGGAATGGCTGCCGCTGGATAAGTGGGTG CCGCAAGTGTTTGTCGCCTCTGGCGATTGCGCCGAGCGTCAGTGGGATTTTTTAGGTCTG GAAATGCCGCAGTGGCTGCTCGGTATTTTTATCGCTTACCTGATTGTCGCAGTGCTGGTG GTGATTTCCCAGCCGTTTAAAGCGAAAAAACGTGATCTGTTCGGTCGCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A6M2 UniProtKB Entry Name DSBB_ECOLI GenBank Protein ID 398018 GenBank Gene ID L03721 - General References
- Bardwell JC, Lee JO, Jander G, Martin N, Belin D, Beckwith J: A pathway for disulfide bond formation in vivo. Proc Natl Acad Sci U S A. 1993 Feb 1;90(3):1038-42. [Article]
- Missiakas D, Georgopoulos C, Raina S: 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 U S A. 1993 Aug 1;90(15):7084-8. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Pinner E, Padan E, Schuldiner S: Cloning, sequencing, and expression of the nhaB gene, encoding a Na+/H+ antiporter in Escherichia coli. J Biol Chem. 1992 Jun 5;267(16):11064-8. [Article]
- Jander G, Martin NL, Beckwith J: Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. EMBO J. 1994 Nov 1;13(21):5121-7. [Article]
- Kobayashi T, Ito K: Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway. EMBO J. 1999 Mar 1;18(5):1192-8. [Article]
- Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G: Global topology analysis of the Escherichia coli inner membrane proteome. Science. 2005 May 27;308(5726):1321-3. [Article]
- Lippa AM, Goulian M: Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli. J Bacteriol. 2012 Mar;194(6):1457-63. doi: 10.1128/JB.06055-11. Epub 2012 Jan 20. [Article]