Difference between revisions of "PrsA"

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* '''Description:''' post-translocational folding of exported proteins (post-translocation molecular chaperone) <br/><br/>
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* '''Description:''' lipoprotein, post-translocational folding of exported proteins (post-translocation molecular chaperone) <br/><br/>
 
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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''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}}
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* '''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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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
 
** PrsA is a lipoprotein with a N-acetyl-S-diacyl-glyceryl-cysteine structure {{PubMed|22303020}}
 
** PrsA is a lipoprotein with a N-acetyl-S-diacyl-glyceryl-cysteine structure {{PubMed|22303020}}
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=prsA_1070364_1071242_-1 prsA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=prsA_1070364_1071242_-1 prsA] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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* '''Additional information:'''
 
* '''Additional information:'''
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** [[PrsA]] is subject to degradation by [[WprA]] and other extracellular proteases {{PubMed|24362423}}
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
  
<pubmed>12634326,14976191,11807061,10096076,18763711, 10871614 20487272 22303020</pubmed>
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<pubmed>12634326,14976191,11807061,10096076,18763711, 10871614 20487272 22303020 24362423 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:28, 16 January 2014

  • Description: lipoprotein, 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
Gene expression levels in SubtiExpress: prsA
Interactions involving this protein in SubtInteract: PrsA
Metabolic function and regulation of this protein in SubtiPathways:
Protein secretion
MW, pI 32 kDa, 9.122
Gene length, protein length 876 bp, 292 aa
Immediate neighbours yhaL, sscA
Sequences Protein DNA DNA_with_flanks
Genetic context
PrsA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PrsA expression.png















Categories containing this gene/protein

protein secretion, essential genes, membrane proteins

This gene is a member of the following regulons

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:
  • Modification:
    • PrsA is a lipoprotein with a N-acetyl-S-diacyl-glyceryl-cysteine structure PubMed
  • Effectors of protein activity:
  • Localization:
    • membrane associated (lipoprotein) 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:
    • PrsA is subject to degradation by WprA and other extracellular proteases PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Laxmi Krishnappa, Carmine G Monteferrante, Jolanda Neef, Annette Dreisbach, Jan Maarten van Dijl
Degradation of extracytoplasmic catalysts for protein folding in Bacillus subtilis.
Appl Environ Microbiol: 2014, 80(4);1463-8
[PubMed:24362423] [WorldCat.org] [DOI] (I p)

Kenji Kurokawa, Kyoung-Hwa Ryu, Rie Ichikawa, Akiko Masuda, Min-Su Kim, Hanna Lee, Jun-Ho Chae, Takashi Shimizu, Tatsuya Saitoh, Koichi Kuwano, Shizuo Akira, Naoshi Dohmae, Hiroshi Nakayama, Bok Luel Lee
Novel bacterial lipoprotein structures conserved in low-GC content gram-positive bacteria are recognized by Toll-like receptor 2.
J Biol Chem: 2012, 287(16);13170-81
[PubMed:22303020] [WorldCat.org] [DOI] (I p)

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)