RegulonDB RegulonDB 10.8: Gene Form
   

cnoX gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

cnoX ybbO fetB fetA tesA anti-anti-terminator anti-terminator terminator TSS_663 TSS_663 ybbNp2 ybbNp2 ybbNp1 ybbNp1 TSS_662 (cluster) TSS_662 (cluster) TSS_661 TSS_661

Gene      
Name: cnoX    Texpresso search in the literature
Synonym(s): ECK0486, G6268, b0492, ybbN
Genome position(nucleotides): 517425 <-- 518279 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
55.91
External database links:  
ASAP:
ABE-0001707
ECHOBASE:
EB3049
OU-MICROARRAY:
b0492
PortEco:
ybbN
STRING:
511145.b0492
COLOMBOS: cnoX


Product      
Name: chaperedoxin
Synonym(s): CnoX, Trxsc, YbbN
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 31.791
Isoelectric point: 4.228
Motif(s):
 
Type Positions Sequence
2 -> 111 SVENIVNINESNLQQVLEQSMTTPVLFYFWSERSQHCLQLTPILESLAAQYNGQFILAKLDCDAEQMIAAQFGLRAIPTVYLFQNGQPVDGFQGPQPEEAIRALLDKVLP
6 -> 107 IVNINESNLQQVLEQSMTTPVLFYFWSERSQHCLQLTPILESLAAQYNGQFILAKLDCDAEQMIAAQFGLRAIPTVYLFQNGQPVDGFQGPQPEEAIRALLD
63 -> 63 C
38 -> 38 C
124 -> 190 LMQESNYTDALPLLKDAWQLSNQNGEIGLLLAETLIALNRSEDAEAVLKTIPLQDQDTRYQGLVAQI

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.4 - chaperoning, repair (refolding)
Gene Ontology Terms (GO)  
cellular_component GO:0005623 - cell
GO:0005829 - cytosol
molecular_function GO:0005515 - protein binding
GO:0051082 - unfolded protein binding
biological_process GO:0042026 - protein refolding
GO:0045454 - cell redox homeostasis
GO:0034599 - cellular response to oxidative stress
GO:0061077 - chaperone-mediated protein folding
GO:0036506 - maintenance of unfolded protein
Note(s): Note(s): ...[more].
Evidence: [APPH] Assay of protein purified to homogeneity
Reference(s): [1] Goemans CV., et al., 2018
[2] Kthiri F., et al., 2008
[3] Le HT., et al., 2011
[4] Lin J., et al., 2011
External database links:  
DIP:
DIP-11322N
ECOCYC:
G6268-MONOMER
ECOLIWIKI:
b0492
INTERPRO:
IPR013766
INTERPRO:
IPR036249
INTERPRO:
IPR011990
MINT:
MINT-1222054
MODBASE:
P77395
PANTHER:
PTHR10438
PDB:
3QOU
PFAM:
PF00085
PRIDE:
P77395
PROSITE:
PS51352
REFSEQ:
NP_415025
SMR:
P77395
SWISSMODEL:
P77395
UNIPROT:
P77395


Operon      
Name: cnoX         
Operon arrangement:
Transcription unit        Promoter
ybbN


RNA cis-regulatory element    
Attenuation: Transcriptional


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_661 518264 reverse nd [RS-EPT-CBR] [5]
  promoter TSS_662 (cluster) 518306 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [5]
  promoter ybbNp2 518568 reverse The sigma factor was determined
Read more >
[AIPP] [6]
  promoter TSS_663 518661 reverse nd [RS-EPT-CBR] [5]


Evidence    

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

 [AIPP] Automated inference of promoter position



Reference(s)    

 [1] Goemans CV., Vertommen D., Agrebi R., Collet JF., 2018, CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation., Mol Cell 70(4):614-627.e7

 [2] Kthiri F., Le HT., Tagourti J., Kern R., Malki A., Caldas T., Abdallah J., Landoulsi A., Richarme G., 2008, The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase., Biochem Biophys Res Commun 374(4):668-72

 [3] Le HT., Gautier V., Kthiri F., Kohiyama M., Katayama T., Richarme G., 2011, DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN., Biochem Biophys Res Commun 405(1):52-7

 [4] Lin J., Wilson MA., 2011, Escherichia coli thioredoxin-like protein YbbN contains an atypical tetratricopeptide repeat motif and is a negative regulator of GroEL., J Biol Chem 286(22):19459-69

 [5] 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.

 [6] Zhao K., Liu M., Burgess RR., 2005, The global transcriptional response of Escherichia coli to induced sigma 32 protein involves sigma 32 regulon activation followed by inactivation and degradation of sigma 32 in vivo., J Biol Chem 280(18):17758-68


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