RegulonDB RegulonDB 10.8: Gene Form
   

dsbB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

nhaB umuC dsbB dsbBp6 dsbBp6

Gene      
Name: dsbB    Texpresso search in the literature
Synonym(s): ECK1173, EG11393, b1185, dsbX, iarB, rosB, roxB, ycgA
Genome position(nucleotides): 1232500 <-- 1233030 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
52.73
External database links:  
ASAP:
ABE-0003979
CGSC:
31933
ECHOBASE:
EB1366
OU-MICROARRAY:
b1185
PortEco:
dsbB
STRING:
511145.b1185
COLOMBOS: dsbB


Product      
Name: protein thiol:quinone oxidoreductase DsbB
Synonym(s): DsbB, DsbX, IarB, RosB, RoxB, YcgA, quinone reductase DsbB
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane
Molecular weight: 20.142
Isoelectric point: 8.595
Motif(s):
 
Type Positions Sequence
44 -> 44 C
118 -> 118 K
145 -> 163 WLLGIFIAYLIVAVLVVIS
12 -> 159 RGAWLLMAFTALALELTALWFQHVMLLKPCVLCIYERCALFGVLGAALIGAIAPKTPLRYVAMVIWLYSAFRGVQLTYEHTMLQLYPSPFATCDFMVRFPEWLPLDKWVPQVFVASGDCAERQWDFLGLEMPQWLLGIFIAYLIVAVL
50 -> 65 ALFGVLGAALIGAIAP

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.3 - posttranslational modification
  6 - cell structure --> 6.1 - membrane
Gene Ontology Terms (GO)  
cellular_component GO:0016020 - membrane
GO:0005886 - plasma membrane
GO:0005887 - integral component of plasma membrane
GO:0016021 - integral component of membrane
molecular_function GO:0005515 - protein binding
GO:0009055 - electron transfer activity
GO:0016491 - oxidoreductase activity
GO:0015035 - protein disulfide oxidoreductase activity
GO:0048039 - ubiquinone binding
GO:0016672 - oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
biological_process GO:0006457 - protein folding
GO:0009408 - response to heat
GO:0022900 - electron transport chain
GO:0055114 - oxidation-reduction process
Note(s): Note(s): ...[more].
Reference(s): [1] Halili MA., et al., 2015
[2] Inaba K., et al., 2005
[3] Kishigami S., et al., 1995
[4] Landeta C., et al., 2017
[5] Malojcic G., et al., 2008
[6] Mizrachi D., et al., 2017
[7] Sperling LJ., et al., 2013
[8] Tang M., et al., 2011
[9] Tapley TL., et al., 2007
[10] Whitley P., et al., 1993
[11] Zhao Z., et al., 2015
External database links:  
ECOCYC:
DSBBPROT-MONOMER
ECOLIWIKI:
b1185
INTERPRO:
IPR003752
INTERPRO:
IPR023380
INTERPRO:
IPR022920
MINT:
P0A6M2
PDB:
3E9J
PDB:
2ZUQ
PDB:
2ZUP
PDB:
2LEG
PDB:
2K74
PDB:
2K73
PDB:
2HI7
PDB:
2LTQ
PFAM:
PF02600
PRIDE:
P0A6M2
PRODB:
PRO_000022480
REFSEQ:
NP_415703
SMR:
P0A6M2
UNIPROT:
P0A6M2


Operon      
Name: dsbB         
Operon arrangement:
Transcription unit        Promoter
 


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter dsbBp6 1233147 reverse Similarity to the consensus
Read more >
[ICWHO] [12]


Evidence    

 [ICWHO] Inferred computationally without human oversight



Reference(s)    

 [1] Halili MA., Bachu P., Lindahl F., Bechara C., Mohanty B., Reid RC., Scanlon MJ., Robinson CV., Fairlie DP., Martin JL., 2015, Small molecule inhibitors of disulfide bond formation by the bacterial DsbA-DsbB dual enzyme system., ACS Chem Biol 10(4):957-64

 [2] Inaba K., Takahashi YH., Ito K., 2005, Reactivities of quinone-free DsbB from Escherichia coli., J Biol Chem 280(38):33035-44

 [3] Kishigami S., Kanaya E., Kikuchi M., Ito K., 1995, DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA., J Biol Chem 270(29):17072-4

 [4] Landeta C., Meehan BM., McPartland L., Ingendahl L., Hatahet F., Tran NQ., Boyd D., Beckwith J., 2017, Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions., J Biol Chem 292(16):6529-6541

 [5] Malojcic G., Owen RL., Grimshaw JP., Glockshuber R., 2008, Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB., FEBS Lett 582(23-24):3301-7

 [6] Mizrachi D., Robinson MP., Ren G., Ke N., Berkmen M., DeLisa MP., 2017, A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo., Nat Chem Biol 13(9):1022-1028

 [7] Sperling LJ., Tang M., Berthold DA., Nesbitt AE., Gennis RB., Rienstra CM., 2013, Solid-state NMR study of a 41 kDa membrane protein complex DsbA/DsbB., J Phys Chem B 117(20):6052-60

 [8] Tang M., Sperling LJ., Berthold DA., Nesbitt AE., Gennis RB., Rienstra CM., 2011, Solid-state NMR study of the charge-transfer complex between ubiquinone-8 and disulfide bond generating membrane protein DsbB., J Am Chem Soc 133(12):4359-66

 [9] Tapley TL., Eichner T., Gleiter S., Ballou DP., Bardwell JC., 2007, Kinetic characterization of the disulfide bond-forming enzyme DsbB., J Biol Chem 282(14):10263-71

 [10] Whitley P., von Heijne G., 1993, The DsbA-DsbB system affects the formation of disulfide bonds in periplasmic but not in intramembraneous protein domains., FEBS Lett 332(1-2):49-51

 [11] Zhao Z., Eberhart LJ., Orfe LH., Lu SY., Besser TE., Call DR., 2015, Genome-Wide Screening Identifies Six Genes That Are Associated with Susceptibility to Escherichia coli Microcin PDI., Appl Environ Microbiol 81(20):6953-63

 [12] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78


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