RegulonDB RegulonDB 11.1: Gene Form
   

torD gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

torA torC torD cbpM

Gene      
Name: torD    Texpresso search in the literature
Synonym(s): ECK0989, EG12195, b0998
Genome position(nucleotides): 1061799 --> 1062398
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 53.33
External database links:  
ASAP:
 ABE-0003374
CGSC:
 29980
ECHOBASE:
 EB2112
ECOLIHUB:
 torD
OU-MICROARRAY:
 b0998
STRING:
 511145.b0998
COLOMBOS: torD


Product      
Name: trimethylamine-N-oxide reductase-specific chaperone
Synonym(s): TorD
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 22.574
Isoelectric point: 4.482
Motif(s):
 
Type Positions Sequence Comment
46 -> 46 S UniProt: In Ref. 1; CAA52096..
49 -> 170 PLTAAVNELENRIATLTVRDDARLELAADFCGLFLMTDKQAALPYASAYKQDEQEIKRLLVEAGMETSGNFNEPADHLAIYLELLSHLHFSLGEGTVPARRIDSLRQKTLTALWQWLPEFVA

 
Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.4 - chaperoning, repair (refolding)
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0005515 - protein binding
GO:0042277 - peptide binding
GO:0042802 - identical protein binding
GO:0043546 - molybdopterin cofactor binding
biological_process GO:0006457 - protein folding
GO:0051604 - protein maturation
GO:0051259 - protein complex oligomerization
Note(s): Note(s): ...[more].
Evidence: [EXP] Inferred from experiment
Reference(s): [1] Bageshwar UK., et al., 2021
[2] Chan CS., et al., 2014
[3] Chan CS., et al., 2010
[4] Dow JM., et al., 2013
[5] Genest O., et al., 2009
[6] Genest O., et al., 2008
[7] Genest O., et al., 2006
[8] Genest O., et al., 2006
[9] Guymer D., et al., 2010
[10] Hatzixanthis K., et al., 2005
[11] Ilbert M., et al., 2003
[12] Jack RL., et al., 2004
[13] Li SY., et al., 2006
[14] Redelberger D., et al., 2013
[15] Turner RJ., et al., 2004
External database links:  
ALPHAFOLD:
 P36662
DIP:
 DIP-11015N
ECOCYC:
 EG12195-MONOMER
ECOLIWIKI:
 b0998
INTERPRO:
 IPR023069
INTERPRO:
 IPR036386
INTERPRO:
 IPR020945
INTERPRO:
 IPR036411
MINT:
 P36662
MODBASE:
 P36662
PFAM:
 PF02613
PRIDE:
 P36662
PRODB:
 PRO_000024087
REFSEQ:
 NP_415518
SMR:
 P36662
SWISSMODEL:
 P36662
UNIPROT:
 P36662


Operon      
Name: torCAD         
Operon arrangement:
Transcription unit        Promoter
torCAD


Transcriptional Regulation      
Display Regulation             
Activated by: TorR
Repressed by: NarL


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


Reference(s)    

 [1] Bageshwar UK., DattaGupta A., Musser SM., 2021, Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation., PLoS One 16(9):e0256715

 [2] Chan CS., Bay DC., Leach TG., Winstone TM., Kuzniatsova L., Tran VA., Turner RJ., 2014, 'Come into the fold': A comparative analysis of bacterial redox enzyme maturation protein members of the NarJ subfamily., Biochim Biophys Acta 1838(12):2971-2984

 [3] Chan CS., Chang L., Winstone TM., Turner RJ., 2010, Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates., FEBS Lett 584(22):4553-8

 [4] Dow JM., Gabel F., Sargent F., Palmer T., 2013, Characterization of a pre-export enzyme-chaperone complex on the twin-arginine transport pathway., Biochem J 452(1):57-66

 [5] Genest O., Mejean V., Iobbi-Nivol C., 2009, Multiple roles of TorD-like chaperones in the biogenesis of molybdoenzymes., FEMS Microbiol Lett 297(1):1-9

 [6] Genest O., Neumann M., Seduk F., Stocklein W., Mejean V., Leimkuhler S., Iobbi-Nivol C., 2008, Dedicated metallochaperone connects apoenzyme and molybdenum cofactor biosynthesis components., J Biol Chem 283(31):21433-40

 [7] Genest O., Seduk F., Ilbert M., Mejean V., Iobbi-Nivol C., 2006, Signal peptide protection by specific chaperone., Biochem Biophys Res Commun 339(3):991-5

 [8] Genest O., Seduk F., Theraulaz L., Mejean V., Iobbi-Nivol C., 2006, Chaperone protection of immature molybdoenzyme during molybdenum cofactor limitation., FEMS Microbiol Lett 265(1):51-5

 [9] Guymer D., Maillard J., Agacan MF., Brearley CA., Sargent F., 2010, Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading chaperone induced by domain swapping., FEBS J 277(2):511-25

 [10] Hatzixanthis K., Clarke TA., Oubrie A., Richardson DJ., Turner RJ., Sargent F., 2005, Signal peptide-chaperone interactions on the twin-arginine protein transport pathway., Proc Natl Acad Sci U S A 102(24):8460-5

 [11] Ilbert M., Mejean V., Giudici-Orticoni MT., Samama JP., Iobbi-Nivol C., 2003, Involvement of a mate chaperone (TorD) in the maturation pathway of molybdoenzyme TorA., J Biol Chem 278(31):28787-92

 [12] Jack RL., Buchanan G., Dubini A., Hatzixanthis K., Palmer T., Sargent F., 2004, Coordinating assembly and export of complex bacterial proteins., EMBO J 23(20):3962-72

 [13] Li SY., Chang BY., Lin SC., 2006, Coexpression of TorD enhances the transport of GFP via the TAT pathway., J Biotechnol 122(4):412-21

 [14] Redelberger D., Genest O., Arabet D., Mejean V., Ilbert M., Iobbi-Nivol C., 2013, Quality control of a molybdoenzyme by the Lon protease., FEBS Lett 587(24):3935-42

 [15] Turner RJ., Papish AL., Sargent F., 2004, Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)., Can J Microbiol 50(4):225-38

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