RegulonDB RegulonDB 10.10: Gene Form
   

dsbA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

yihF srkA dsbA terminator terminator yihFp1 yihFp1 yihFp6 yihFp6 yihFp4 yihFp4 TSS_4532 TSS_4532 TSS_4531 TSS_4531 TSS_4530 (cluster) TSS_4530 (cluster) dsbAp dsbAp TSS_4528 TSS_4528

Gene      
Name: dsbA    Texpresso search in the literature
Synonym(s): ECK3852, EG11297, b3860, dsf, iarA, ppfA
Genome position(nucleotides): 4043418 --> 4044044 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 48.01
External database links:  
ASAP:
 ABE-0012606
CGSC:
 34063
ECHOBASE:
 EB1274
ECOLIHUB:
 dsbA
OU-MICROARRAY:
 b3860
STRING:
 511145.b3860
COLOMBOS: dsbA


Product      
Name: thiol:disulfide oxidoreductase DsbA
Synonym(s): DsbA, DsbAreduced, Dsf, IarA, PpfA, protein disulfide oxidoreductase DsbA, thiol:disulfide oxidoreductase - DsbAreduced
Sequence: Get amino acid sequence Fasta Format
Cellular location: periplasmic space
Molecular weight: 23.105
Isoelectric point: 6.275
Motif(s):
 
Type Positions Sequence
50 -> 51 PH
1 -> 19 MKKIWLALAGLVLAFSASA
20 -> 150 AQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVV
170 -> 170 P
40 -> 197 QVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQLNPQGMDTSNMDVFVQQY

 
Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.4 - chaperoning, repair (refolding)
  5 - cell processes --> 5.5 - adaptations
Gene Ontology Terms (GO)  
cellular_component GO:0030288 - outer membrane-bounded periplasmic space
GO:0042597 - periplasmic space
molecular_function GO:0003756 - protein disulfide isomerase activity
GO:0005515 - protein binding
GO:0016491 - oxidoreductase activity
GO:0015035 - protein-disulfide reductase activity
biological_process GO:0071236 - cellular response to antibiotic
GO:0018215 - protein phosphopantetheinylation
Note(s): Note(s): ...[more].
Reference(s): [1] Beld J., et al., 2010
[2] Bessette PH., et al., 2001
[3] Carvalho AT., et al., 2006
[4] Couprie J., et al., 2000
[5] Fabianek RA., et al., 2000
[6] Frech C., et al., 1995
[7] Frech C., et al., 1996
[8] Hennecke J., et al., 1997
[9] Joly JC., et al., 1994
[10] Jonda S., et al., 1999
[11] Manjasetty BA., et al., 2004
[12] Maskos K., et al., 2003
[13] Messens J., et al., 2007
[14] Moutiez M., et al., 1999
[15] Ondo-Mbele E., et al., 2005
[16] Regeimbal J., et al., 2002
[17] Schirra HJ., et al., 1998
[18] Shouldice SR., et al., 2010
[19] Sone M., et al., 1997
[20] Wunderlich M., et al., 1993
[21] Wunderlich M., et al., 1993
[22] Wunderlich M., et al., 1993
[23] Zapun A., et al., 1994
[24] Zhao Z., et al., 2015
External database links:  
DIP:
 DIP-35886N
ECOCYC:
 DISULFOXRED-MONOMER
ECOLIWIKI:
 b3860
INTERPRO:
 IPR023205
INTERPRO:
 IPR036249
INTERPRO:
 IPR001853
INTERPRO:
 IPR013766
INTERPRO:
 IPR017937
MINT:
 P0AEG4
MODBASE:
 P0AEG4
PDB:
 1FVK
PDB:
 6PVZ
PDB:
 6PVY
PDB:
 6POQ
PDB:
 6POI
PDB:
 6POH
PDB:
 6PML
PDB:
 6PMF
PDB:
 6PLI
PDB:
 1A23
PDB:
 1A24
PDB:
 1A2J
PDB:
 1A2L
PDB:
 1A2M
PDB:
 1AC1
PDB:
 1ACV
PDB:
 1BQ7
PDB:
 1DSB
PDB:
 1FVJ
PDB:
 1TI1
PDB:
 1U3A
PDB:
 1UN2
PDB:
 2B3S
PDB:
 2B6M
PDB:
 2HI7
PDB:
 2LEG
PDB:
 2NDO
PDB:
 2ZUP
PDB:
 3E9J
PDB:
 4TKY
PDB:
 4ZIJ
PDB:
 6BQX
PDB:
 6BR4
PDB:
 6PBI
PDB:
 6PC9
PDB:
 6PD7
PDB:
 6PDH
PDB:
 6PG2
PDB:
 6PGJ
PFAM:
 PF01323
PRIDE:
 P0AEG4
PRODB:
 PRO_000022479
PROSITE:
 PS51352
PROSITE:
 PS00194
REFSEQ:
 NP_418297
SMR:
 P0AEG4
SWISSMODEL:
 P0AEG4
UNIPROT:
 P0AEG4


Operon      
Name: srkA-dsbA         
Operon arrangement:
Transcription unit        Promoter
srkA-dsbA
dsbA


Transcriptional Regulation      
Display Regulation             
Activated by: CpxR


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 TSS_4528 4043252 forward nd [RS-EPT-CBR] [25]
  promoter TSS_4530 (cluster) 4043383 forward nd [RS-EPT-CBR] [25]
  promoter TSS_4531 4043393 forward nd [RS-EPT-CBR] [25]
  promoter TSS_4532 4043397 forward nd [RS-EPT-CBR] [25]
  promoter yihFp4 4044055 forward nd [ICWHO] [26]
  promoter yihFp6 4044131 forward nd [ICWHO] [26]
  promoter yihFp1 4044175 forward nd [ICWHO] [26]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

 [ICWHO] Inferred computationally without human oversight


Reference(s)    

 [1] Beld J., Woycechowsky KJ., Hilvert D., 2010, Small-molecule diselenides catalyze oxidative protein folding in vivo., ACS Chem Biol 5(2):177-82

 [2] Bessette PH., Qiu J., Bardwell JC., Swartz JR., Georgiou G., 2001, Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli., J Bacteriol 183(3):980-8

 [3] Carvalho AT., Fernandes PA., Ramos MJ., 2006, Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA., J Comput Chem 27(8):966-75

 [4] Couprie J., Vinci F., Dugave C., Quemeneur E., Moutiez M., 2000, Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex., Biochemistry 39(22):6732-42

 [5] Fabianek RA., Hennecke H., Thony-Meyer L., 2000, Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli., FEMS Microbiol Rev 24(3):303-16

 [6] Frech C., Schmid FX., 1995, DsbA-mediated disulfide bond formation and catalyzed prolyl isomerization in oxidative protein folding., J Biol Chem 270(10):5367-74

 [7] Frech C., Wunderlich M., Glockshuber R., Schmid FX., 1996, Preferential binding of an unfolded protein to DsbA., EMBO J 15(2):392-98

 [8] Hennecke J., Spleiss C., Glockshuber R., 1997, Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA., J Biol Chem 272(1):189-95

 [9] Joly JC., Swartz JR., 1994, Protein folding activities of Escherichia coli protein disulfide isomerase., Biochemistry 33(14):4231-6

 [10] Jonda S., Huber-Wunderlich M., Glockshuber R., Mossner E., 1999, Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm., EMBO J 18(12):3271-81

 [11] Manjasetty BA., Hennecke J., Glockshuber R., Heinemann U., 2004, Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments., Acta Crystallogr D Biol Crystallogr 60(Pt 2):304-9

 [12] Maskos K., Huber-Wunderlich M., Glockshuber R., 2003, DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo., J Mol Biol 325(3):495-513

 [13] Messens J., Collet JF., Van Belle K., Brosens E., Loris R., Wyns L., 2007, The oxidase DsbA folds a protein with a nonconsecutive disulfide., J Biol Chem 282(43):31302-7

 [14] Moutiez M., Burova TV., Haertle T., Quemeneur E., 1999, On the non-respect of the thermodynamic cycle by DsbA variants., Protein Sci 8(1):106-12

 [15] Ondo-Mbele E., Vives C., Kone A., Serre L., 2005, Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant., J Mol Biol 347(3):555-63

 [16] Regeimbal J., Bardwell JC., 2002, DsbB catalyzes disulfide bond formation de novo., J Biol Chem 277(36):32706-13

 [17] Schirra HJ., Renner C., Czisch M., Huber-Wunderlich M., Holak TA., Glockshuber R., 1998, Structure of reduced DsbA from Escherichia coli in solution., Biochemistry 37(18):6263-76

 [18] Shouldice SR., Cho SH., Boyd D., Heras B., Eser M., Beckwith J., Riggs P., Martin JL., Berkmen M., 2010, In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling., Mol Microbiol 75(1):13-28

 [19] Sone M., Akiyama Y., Ito K., 1997, Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds., J Biol Chem 272(16):10349-52

 [20] Wunderlich M., Glockshuber R., 1993, In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA)., J Biol Chem 268(33):24547-50

 [21] Wunderlich M., Jaenicke R., Glockshuber R., 1993, The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form., J Mol Biol 233(4):559-66

 [22] Wunderlich M., Otto A., Seckler R., Glockshuber R., 1993, Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH., Biochemistry 32(45):12251-6

 [23] Zapun A., Cooper L., Creighton TE., 1994, Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo., Biochemistry 33(7):1907-14

 [24] 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

 [25] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

 [26] 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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