MG1655
W3110
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Gene Report : dsbA
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)
Arch Microbiol. 1995;164(4):301-7.
An essential role for DsbA in cytochrome c synthesis and formate-dependent nitrite reduction by Escherichia coli K-12.
Metheringham R, Griffiths L, Crooke H, Forsythe S, Cole J. ( 7487336 )
     Deletion OCR05 (D)  ,  OCR05,6-2 (D)  ,  OCR05-12-1 (D)  ,  OCR05-13 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  dsbA
Related strains
     Strains Search Search strains by gene name:  dsbA   Search strains by all related name:  dsbA b3860 dsf ECK3852 iarA JW3832 o208 ppfA

General information  (Go to Linear View:)
 Gene Name dsbA  
 Alternative name b3860,dsf,ECK3852,iarA,JW3832,o208,ppfA  
 Location, Length 4,041,441 - 4,042,067 (  +  ) ;   87.11 min ; 627 (bp) ,   208 (aa) Go to Linear View
 Product periplasmic protein disulfide isomerase I  
 Operon Name rdoA-dsbA  
 Note protein disulfide isomerase I, essential for cytochrome c synthesis and formate-dependent reduction; GO_component: GO:0042597 - periplasmic space; GO_process: GO:0006457 - protein folding; GO_process: GO:0006950 - response to stress  
 Function enzyme; Proteins - translation and modification  
 Gene Ontology GO:0005515; protein binding ( dsbA )
GO:0015035; protein disulfide oxidoreductase activity ( dsbA )
GO:0030288; outer membrane-bounded periplasmic space ( dsbA )
GO:0042597; periplasmic space ( dsbA )
GO:0045454; cell redox homeostasis ( dsbA )
 PID 1790291  
 EC number
  (KEGG Pathway)
 
5.3.4.1  
Verified Protein Starts (data compiled from literature and appropriate citations are available from EcoGene)
     EcoGene dsbA ( EG11297 )  
    Number of removed 19 aa cleaved  
SWISS-PROT  ( Show details [ 2 more] )
  botton Entry name(Acc.no) DSBA_ECOLI ( P24991 ; Q46951; Q46952 )
    -  Protein name Thiol:disulfide interchange protein dsbA precursor.  
    -  Synonyms  
    -  Gene name OrderedLocusNames=b3860, z5392, ECs4783;  

 Linear View (Whole Mode)
View Location
   4030.0  –  4055.0 (KBP)

Homology Analysis
BLAST
    Bacteria
         GTOP dsbA (  homologous genes of other bacterias  )  
    PDB     (database updated : 2007.02.20 )
         PSI-BLAST Chain A, Dsba (Disulfide Bond Formation Protein)  
    SWISS-PROT     (database updated : 2007.02.20 )
         BLAST Thiol:disulfide interchange protein dsbA precursor  
         PSI-BLAST Thiol:disulfide interchange protein dsbA precursor
    nr     (database updated : 2007.02.20 )
         BLAST protein disulfide isomerase I, essential for cytochrome c synthesis and formate-dependent reduction [Escherichia coli O157:H7 EDL933]  
Pfam 28.0   (database updated : 2015-05 )
    Pfam
PROSITE
    PROSITE PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    MYRISTYL    THIOREDOXIN     

Other Cross-Reference
    EcoCyc dsbA 

MMBR References
Proc Natl Acad Sci U S A. 1995;92:9895-9899
Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA.
Guilhot, C., G. Jander, N. L. Martin, and J. R. Beckwith.
J Biol Chem. 1995;270:17072-17074
DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA.
Kishigami, S., E. Kanaya, M. Kikuchi, and K. Ito.
Proc Natl Acad Sci U S A. 1993;90:1038-1042
A pathway for disulfide bond formation in vivo.
Bardwell, J. C., J. O. Lee, G. Jander, N. Martin, D. Belin, and J. R. Beckwith.
Cell. 1991;67(3):581-9.
Identification of a protein required for disulfide bond formation in vivo.
Bardwell JC, McGovern K, Beckwith J. ( 1934062 )
Nature. 1993;365(6445):464-8.
Crystal structure of the DsbA protein required for disulphide bond formation in vivo.
Martin JL, Bardwell JC, Kuriyan J. ( 8413591 )
Mol Gen Genet. 1994;242(1):23-32.
A pleiotropic acid phosphatase-deficient mutant of Escherichia coli shows premature termination in the dsbA gene. Use of dsbA::phoA fusions to localize a structurally important domain in DsbA.
Belin P, Quemeneur E, Boquet PL. ( 8277944 )
Arch Microbiol. 1995;164(4):301-7.
An essential role for DsbA in cytochrome c synthesis and formate-dependent nitrite reduction by Escherichia coli K-12.
Metheringham R, Griffiths L, Crooke H, Forsythe S, Cole J. ( 7487336 )
Proc Natl Acad Sci U S A. 1992;89:12058-12062
Translocation of a folded protein across the outer membrane in Escherichia coli.
Pugsley, A. P.
Mol Gen Genet. 1993;237(3):407-11.
A mutation in the dsbA gene coding for periplasmic disulfide oxidoreductase reduces transcription of the Escherichia coli ompF gene.
Pugsley AP. ( 8483456 )
FEBS Lett. 1996;398(2-3):265-8.
Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds.
Sambongi Y, Ferguson SJ. ( 8977120 )
J Biol Chem. 1992;267:22440-22445
In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product.
Akiyama, Y., S. Kamitani, N. Kusukawa, and K. Ito.
J Biol Chem. 1993;268:24547-24550
In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA).
Wunderlich, M., and R. Glockshuber.
J Bacteriol. 1994;176:2906-2913
Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation.
Yamanaka, H., M. Kameyama, T. Baba, Y. Fujii, and K. Okamoto.
J Bacteriol. 1995;177:462-464
A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli.
Alksne, L. E., D. Keeney, and B. A. Rasmussen.
Proc Natl Acad Sci U S A. 1993;90:1043-1047
Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.
Dailey, F. E., and H. C. Berg.

Sequences
Amino acid
FASTA format
0001 MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP HCYQFEEVLH ISDNVKKKLP 
0071 EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA LGVEDKVTVP LFEGVQKTQT IRSASDIRDV FINAGIKGEE 
0141 YDAAWNSFVV KSLVAQQEKA AADVQLRGVP AMFVNGKYQL NPQGMDTSNM DVFVQQYADT VKYLSEKK

Nucleotide
FASTA format

View sequence out neighbor 100bp
-100                                             TACTGGCTGC GACAGACGGC GACTTTTATA 
-070 GAACAGGCAA AAGTTCTACA AGAACCCCCT TTGCAATTAA CACCTATGTA TTAATCGGAG AGAGTAGATC 
0001 atgaaaaaga tttggctggc gctggctggt ttagttttag cgtttagcgc atcggcggcg cagtatgaag 
0071 atggtaaaca gtacactacc ctggaaaaac cggtagctgg cgcgccgcaa gtgctggagt ttttctcttt 
0141 cttctgcccg cactgctatc agtttgaaga agttctgcat atttctgata atgtgaagaa aaaactgccg 
0211 gaaggcgtga agatgactaa ataccacgtc aacttcatgg gtggtgacct gggcaaagat ctgactcagg 
0281 catgggctgt ggcgatggcg ctgggcgtgg aagacaaagt gactgttccg ctgtttgaag gcgtacagaa 
0351 aacccagacc attcgttctg cttctgatat ccgcgatgta tttatcaacg caggtattaa aggtgaagag 
0421 tacgacgcgg cgtggaacag cttcgtggtg aaatctctgg tcgctcagca ggaaaaagct gcagctgacg 
0491 tgcaattgcg tggcgttccg gcgatgtttg ttaacggtaa atatcagctg aatccgcagg gtatggatac 
0561 cagcaatatg gatgtttttg ttcagcagta tgctgataca gtgaaatatc tgtccgagaa aaaataaTTC 
0631 AATGTAAATT ACATAAAGCC CGTGAATATT CACGGGCTTT TTTTATTATT TAATAAATAT AAATACATTC 
0701 TGATAATGCA TCCTGCCGCT GGACATT