Thiol:disulfide interchange protein dsbD (P36655)

Identification
Name:Thiol:disulfide interchange protein dsbD
Synonyms:
  • C-type cytochrome biogenesis protein cycZ
  • Inner membrane copper tolerance protein
  • Protein-disulfide reductase
  • Disulfide reductase
Gene Name:dsbD
Enzyme Class:
Biological Properties
General Function:Involved in cytochrome complex assembly
Specific Function:Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of dsbC, dsbE and dsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0Protein dithiol+1.0Thumb+1.0Thumb ↔ 1.0Protein disulfide+1.0Thumb+1.0Thumb+1.0Thumb
1.0Protein dithiol + 1.0NAD + 1.0NADP ↔ 1.0Protein disulfide + 1.0NADH + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0fused thiol:disulfide interchange protein (oxidized)+1.0Reduced Thioredoxin → 1.0fused thiol:disulfide interchange protein (reduced)+1.0Oxidized Thioredoxin
1.0fused thiol:disulfide interchange protein (oxidized) + 1.0Reduced Thioredoxin → 1.0fused thiol:disulfide interchange protein (reduced) + 1.0Oxidized Thioredoxin
ReactionCard
1.0fused thiol:disulfide interchange protein (reduced)+1.0protein disulfide isomerase II (oxidized) → 1.0fused thiol:disulfide interchange protein (oxidized)+1.0protein disulfide isomerase II (reduced)
1.0fused thiol:disulfide interchange protein (reduced) + 1.0protein disulfide isomerase II (oxidized) → 1.0fused thiol:disulfide interchange protein (oxidized) + 1.0protein disulfide isomerase II (reduced)
ReactionCard
1.0fused thiol:disulfide interchange protein (reduced)+1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (oxidized) → 1.0fused thiol:disulfide interchange protein (oxidized)+1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (reduced)
1.0fused thiol:disulfide interchange protein (reduced) + 1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (oxidized) → 1.0fused thiol:disulfide interchange protein (oxidized) + 1.0periplasmic disulfide isomerase/thiol-disulphide oxidase (reduced)
ReactionCard
1.0Protein dithiol+1.0NAD(P)(+) → 1.0protein disulfide+1.0NAD(P)H
1.0Protein dithiol + 1.0NAD(P)(+) → 1.0protein disulfide + 1.0NAD(P)H
ReactionCard
Metabolites:
ECMDB IDNameView
GO Classification:
Component
cell part
membrane
Process
cell redox homeostasis
cellular component assembly
cellular component organization
cellular component organization or biogenesis
cellular homeostasis
cellular process
cellular protein complex assembly
cytochrome complex assembly
macromolecular complex assembly
metabolic process
oxidation reduction
protein complex assembly
Gene Properties
Blattner:b4136
Gene OrientationCounterclockwise
Centisome Percentage:94.00
Left Sequence End4361368
Right Sequence End4363065
Gene Sequence:
>1698 bp
GTGCACGAAATATTCAACATGCTGCTGGCGGTCTTCGATCGGGCAGCGTTAATGCTTATC
TGCCTGTTCTTTCTCATCCGTATCCGCCTGTTTCGCGAACTGTTGCACAAGTCGGCGCAC
TCCCCAAAAGAATTGCTCGCCGTTACCGCCATTTTCTCGCTGTTCGCCCTGTTCAGCACC
TGGTCCGGCGTTCCCGTAGAAGGCTCGCTGGTGAACGTACGTATTATCGCGGTGATGTCC
GGCGGGATTCTGTTTGGCCCGTGGGTAGGCATCATTACCGGCGTGATTGCGGGTATTCAC
CGGTATTTAATTGATATCGGCGGCGTGACGGCGATCCCCTGCTTTATCACCAGCATTCTG
GCGGGTTGTATATCGGGCTGGATCAACCTGAAAATCCCCAAAGCACAGCGCTGGCGCGTC
GGTATTCTCGGCGGCATGTTGTGTGAGACGTTGACCATGATTCTGGTAATTGTCTGGGCA
CCAACTACCGCGTTGGGGATCGATATCGTCTCTAAAATCGGCATTCCAATGATCCTCGGT
AGCGTCTGTATCGGCTTTATTGTGCTTCTGGTGCAAAGCGTTGAGGGCGAAAAAGAGGCC
AGCGCCGCGCGGCAGGCCAAGCTGGCGCTGGATATCGCCAACAAAACGCTACCGCTGTTT
CGCCATGTCAATAGCGAGTCATTACGCAAGGTCTGCGAAATTATCCGCGATGACATTCAC
GCCGATGCGGTGGCGATTACTAATACCGATCATGTGCTGGCCTATGTTGGCGTGGGTGAA
CATAACTATCAGAATGGCGATGACTTCATTAGCCCGACTACCCGTCAGGCGATGAATTAC
GGAAAAATCATCATTAAAAACAATGATGAAGCCCACCGCACACCAGAGATTCATTCCATG
CTGGTGATCCCATTGTGGGAGAAAGGGGTCGTGACCGGAACGCTGAAAATTTACTACTGC
CACGCGCATCAGATCACCTCGTCATTACAGGAAATGGCGGTCGGTCTGTCGCAAATCATC
TCCACGCAACTGGAGGTTTCACGCGCCGAGCAGCTACGTGAAATGGCAAATAAGGCAGAG
CTTCGCGCCCTGCAAAGCAAAATTAATCCCCATTTTCTGTTTAACGCTCTGAACGCTATT
TCATCGTCAATCCGTCTGAATCCGGATACCGCTCGCCAGTTGATCTTTAATCTGTCGCGT
TATCTGCGCTATAACATTGAATTAAAAGACGATGAGCAAATCGATATCAAAAAAGAGCTG
TATCAAATTAAAGACTATATTGCCATTGAGCAGGCCCGCTTTGGTGACAAGCTGACGGTT
ATCTATGATATTGATGAAGAGGTGAATTGCTGCATTCCCAGCCTGCTGATCCAGCCGTTG
GTGGAGAACGCCATTGTCCACGGTATTCAGCCTTGCAAAGGTAAAGGCGTTGTCACCATC
AGCGTTGCAGAGTGCGGAAATCGGGTACGCATTGCGGTGCGAGATACCGGGCACGGCATC
GATCCAAAGGTGATTGAGCGGGTCGAAGCGAATGAAATGCCGGGCAATAAAATTGGCCTG
CTGAATGTCCATCATCGCGTGAAGTTATTGTATGGCGAGGGGCTGCATATCCGCCGCCTG
GAGCCGGGGACGGAAATTGCGTTTTACATTCCTAACCAACGCACCCCAGTCGCCTCACAG
GCTACGTTATTGCTTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:565
Protein Molecular Weight:61795
Protein Theoretical pI:7
PDB File:1SE1
Signaling Regions:
  • 1-19
Transmembrane Regions:
  • 163-183
  • 208-228
  • 243-263
  • 296-316
  • 323-343
  • 357-377
  • 384-404
  • 418-438
Protein Sequence:
>Thiol:disulfide interchange protein dsbD
MAQRIFTLILLLCSTSVFAGLFDAPGRSQFVPADQAFAFDFQQNQHDLNLTWQIKDGYYL
YRKQIRITPEHAKIADVQLPQGVWHEDEFYGKSEIYRDRLTLPVTINQASAGATLTVTYQ
GCADAGFCYPPETKTVPLSEVVANNAAPQPVSVPQQEQPTAQLPFSALWALLIGIGIAFT
PCVLPMYPLISGIVLGGKQRLSTARALLLTFIYVQGMALTYTALGLVVAAAGLQFQAALQ
HPYVLIGLAIVFTLLAMSMFGLFTLQLPSSLQTRLTLMSNRQQGGSPGGVFVMGAIAGLI
CSPCTTAPLSAILLYIAQSGNMWLGGGTLYLYALGMGLPLMLITVFGNRLLPKSGPWMEQ
VKTAFGFVILALPVFLLERVIGDVWGLRLWSALGVAFFGWAFITSLQAKRGWMRIVQIIL
LAAALVSVRPLQDWAFGATHTAQTQTHLNFTQIKTVDELNQALVEAKGKPVMLDLYADWC
VACKEFEKYTFSDPQVQKALADTVLLQANVTANDAQDVALLKHLNVLGLPTILFFDGQGQ
EHPQARVTGFMDAETFSAHLRDRQP
References
External Links:
ResourceLink
Uniprot ID:P36655
Uniprot Name:DSBD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675386
PDB ID:1SE1
Ecogene ID:EG12178
Ecocyc:EG12178
ColiBase:b4136
Kegg Gene:b4136
EchoBASE ID:EB2095
CCDB:DSBD_ECOLI
BacMap:16131961
General Reference:
  • 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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Chung, J., Chen, T., Missiakas, D. (2000). "Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm." Mol Microbiol 35:1099-1109. Pubmed: 10712691
  • Crooke, H., Cole, J. (1995). "The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain." Mol Microbiol 15:1139-1150. Pubmed: 7623667
  • 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
  • Fong, S. T., Camakaris, J., Lee, B. T. (1995). "Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12." Mol Microbiol 15:1127-1137. Pubmed: 7623666
  • Gordon, E. H., Page, M. D., Willis, A. C., Ferguson, S. J. (2000). "Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function." Mol Microbiol 35:1360-1374. Pubmed: 10760137
  • 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
  • Katzen, F., Beckwith, J. (2000). "Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade." Cell 103:769-779. Pubmed: 11114333
  • Krupp, R., Chan, C., Missiakas, D. (2001). "DsbD-catalyzed transport of electrons across the membrane of Escherichia coli." J Biol Chem 276:3696-3701. Pubmed: 11085993
  • Missiakas, D., Schwager, F., Raina, S. (1995). "Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli." EMBO J 14:3415-3424. Pubmed: 7628442
  • Sambongi, Y., Ferguson, S. J. (1994). "Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein." FEBS Lett 353:235-238. Pubmed: 7957865
  • Stewart, E. J., Katzen, F., Beckwith, J. (1999). "Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli." EMBO J 18:5963-5971. Pubmed: 10545108