Difference between revisions of "PrsA"

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* '''Description:''' protein secretion (post-translocation molecular chaperone) <br/><br/>
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* '''Description:''' post-translocational folding of exported proteins (post-translocation molecular chaperone) <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || post-translocation molecular chaperone
 
|style="background:#ABCDEF;" align="center"| '''Product''' || post-translocation molecular chaperone
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || protein secretion
+
|style="background:#ABCDEF;" align="center"|'''Function''' || protein folding
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 32 kDa, 9.122   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 32 kDa, 9.122   
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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:''' Peptidylproline (omega=180) = peptidylproline (omega=0) (according to Swiss-Prot)  
+
* '''Catalyzed reaction/ biological activity:''' catalyses the post-translocational folding of exported proteins {{PubMed|20487272}}, required for folding of [[penicillin-binding proteins]] ([[PbpA]], [[PbpB]], [[PbpC]], [[PbpD]]) {{PubMed|20487272}}
  
 
* '''Protein family:''' PpiC domain (according to Swiss-Prot)
 
* '''Protein family:''' PpiC domain (according to Swiss-Prot)
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:'''
+
* '''Interactions:''' dimeric or oligomeric protein {{PubMed|20487272}}
  
* '''Localization:''' cell membrane (according to Swiss-Prot), membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
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* '''Localization:''' membrane associated {{PubMed|18763711,20487272}}, distinct spots organized in a helical pattern along the cell membrane {{PubMed|20487272}}
  
 
=== Database entries ===
 
=== Database entries ===
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=References=
 
=References=
  
<pubmed>12634326,14976191,11807061,10096076,18763711, 10871614 </pubmed>
+
<pubmed>12634326,14976191,11807061,10096076,18763711, 10871614 20487272 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:06, 22 May 2010

  • Description: post-translocational folding of exported proteins (post-translocation molecular chaperone)

Gene name prsA
Synonyms
Essential yes PubMed
Product post-translocation molecular chaperone
Function protein folding
MW, pI 32 kDa, 9.122
Gene length, protein length 876 bp, 292 aa
Immediate neighbours yhaL, yhzE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PrsA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU09950

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Protein family: PpiC domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions: dimeric or oligomeric protein PubMed
  • Localization: membrane associated PubMed, distinct spots organized in a helical pattern along the cell membrane PubMed

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Hanne-Leena Hyyryläinen, Bogumila C Marciniak, Kathleen Dahncke, Milla Pietiäinen, Pascal Courtin, Marika Vitikainen, Raili Seppala, Andreas Otto, Dörte Becher, Marie-Pierre Chapot-Chartier, Oscar P Kuipers, Vesa P Kontinen
Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis.
Mol Microbiol: 2010, 77(1);108-27
[PubMed:20487272] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Marika Vitikainen, Ilkka Lappalainen, Raili Seppala, Haike Antelmann, Harry Boer, Suvi Taira, Harri Savilahti, Michael Hecker, Mauno Vihinen, Matti Sarvas, Vesa P Kontinen
Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis.
J Biol Chem: 2004, 279(18);19302-14
[PubMed:14976191] [WorldCat.org] [DOI] (P p)

Eva Wahlström, Marika Vitikainen, Vesa P Kontinen, Matti Sarvas
The extracytoplasmic folding factor PrsA is required for protein secretion only in the presence of the cell wall in Bacillus subtilis.
Microbiology (Reading): 2003, 149(Pt 3);569-577
[PubMed:12634326] [WorldCat.org] [DOI] (P p)

Tiina Pummi, Soile Leskelä, Eva Wahlström, Ulf Gerth, Harold Tjalsma, Michael Hecker, Matti Sarvas, Vesa P Kontinen
ClpXP protease regulates the signal peptide cleavage of secretory preproteins in Bacillus subtilis with a mechanism distinct from that of the Ecs ABC transporter.
J Bacteriol: 2002, 184(4);1010-8
[PubMed:11807061] [WorldCat.org] [DOI] (P p)

H L Hyyrylainen, M Vitikainen, J Thwaite, H Wu, M Sarvas, C R Harwood, V P Kontinen, K Stephenson
D-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis.
J Biol Chem: 2000, 275(35);26696-703
[PubMed:10871614] [WorldCat.org] [DOI] (P p)

S Leskelä, E Wahlström, V P Kontinen, M Sarvas
Lipid modification of prelipoproteins is dispensable for growth but essential for efficient protein secretion in Bacillus subtilis: characterization of the Lgt gene.
Mol Microbiol: 1999, 31(4);1075-85
[PubMed:10096076] [WorldCat.org] [DOI] (P p)