Identification
Name:Disulfide bond formation protein B
Synonyms:
  • Disulfide oxidoreductase
Gene Name:dsbB
Enzyme Class:Not Available
Biological Properties
General Function:Involved in 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
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
EcoCyc Reactions:
Protein-Red-DisulfidesProtein-Ox-Disulfides
Protein-Red-Disulfides ↔ Protein-Ox-Disulfides
ReactionCard
Complex Reactions:
Thumb+periplasmic protein disulfide isomerase I (reduced)Thumb+periplasmic protein disulfide isomerase I (oxidized)
Ubiquinone-8 + periplasmic protein disulfide isomerase I (reduced) → Ubiquinol-8 + periplasmic protein disulfide isomerase I (oxidized)
ReactionCard
Menaquinone 8+periplasmic protein disulfide isomerase I (reduced)Thumb+periplasmic protein disulfide isomerase I (oxidized)
Menaquinone 8 + periplasmic protein disulfide isomerase I (reduced) → Menaquinol 8 + periplasmic protein disulfide isomerase I (oxidized)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21245Menaquinol 8MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
GO Classification:
Component
cell part
membrane
Function
catalytic activity
disulfide oxidoreductase activity
oxidoreductase activity
oxidoreductase activity, acting on a sulfur group of donors
protein disulfide oxidoreductase activity
Gene Properties
Blattner:b1185
Gene OrientationCounterclockwise
Centisome Percentage:26.55
Left Sequence End1231723
Right Sequence End1232253
Gene Sequence:
>531 bp
ATGATTCTTATAATTTATGCGCATCCGTATCCGCATCATTCCCATGCGAATAAACGGATG
CTTGAACAGGCAAGGACGCTGGAAGGCGTCGAAATTCGCTCTCTTTATCAACTCTATCCT
GACTTCAATATCGATATTGCCGCCGAGCAGGAGGCGCTGTCTCGCGCCGATCTGATCGTC
TGGCAGCATCCGATGCAGTGGTACAGCATTCCTCCGCTCCTCAAACTTTGGATCGATAAA
GTTTTCTCCCACGGCTGGGCTTACGGTCATGGCGGCACGGCGCTGCATGGCAAACATTTG
CTGTGGGCGGTGACGACCGGCGGCGGGGAAAGCCATTTTGAAATTGGTGCGCATCCGGGC
TTTGATGTGCTGTCGCAGCCGCTACAGGCGACGGCAATCTACTGCGGGCTGAACTGGCTG
CCACCGTTTGCCATGCACTGCACCTTTATTTGTGACGACGAAACCCTCGAAGGGCAGGCG
CGTCACTATAAGCAACGTCTGCTGGAATGGCAGGAGGCCCATCATGGATAG
Protein Properties
Pfam Domain Function:
Protein Residues:176
Protein Molecular Weight:20142
Protein Theoretical pI:9
Signaling Regions:
  • None
Transmembrane Regions:
  • 15-31
  • 50-65
  • 72-89
  • 145-163
Protein Sequence:
>Disulfide bond formation protein B
MLRFLNQCSQGRGAWLLMAFTALALELTALWFQHVMLLKPCVLCIYERCALFGVLGAALI
GAIAPKTPLRYVAMVIWLYSAFRGVQLTYEHTMLQLYPSPFATCDFMVRFPEWLPLDKWV
PQVFVASGDCAERQWDFLGLEMPQWLLGIFIAYLIVAVLVVISQPFKAKKRDLFGR
References
External Links:
ResourceLink
Uniprot ID:P0A6M2
Uniprot Name:DSBB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674301
Ecogene ID:EG11393
Ecocyc:EG11393
ColiBase:b1185
Kegg Gene:b1185
EchoBASE ID:EB1366
CCDB:DSBB_ECOLI
BacMap:49176085
General Reference:
  • Bardwell, J. C., Lee, J. O., Jander, G., Martin, N., Belin, D., Beckwith, J. (1993). "A pathway for disulfide bond formation in vivo." Proc Natl Acad Sci U S A 90:1038-1042. Pubmed: 8430071
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jander, G., Martin, N. L., Beckwith, J. (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. Pubmed: 7957076
  • Kobayashi, T., Ito, K. (1999). "Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway." EMBO J 18:1192-1198. Pubmed: 10064586
  • Missiakas, D., Georgopoulos, C., Raina, S. (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 U S A 90:7084-7088. Pubmed: 7688471
  • 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, a. l. .. (1996). "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 3:137-155. Pubmed: 8905232
  • Pinner, E., Padan, E., Schuldiner, S. (1992). "Cloning, sequencing, and expression of the nhaB gene, encoding a Na+/H+ antiporter in Escherichia coli." J Biol Chem 267:11064-11068. Pubmed: 1317851