PrsA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein secretion, essential genes, membrane proteins

The gene

Basic information

• Locus tag: BSU09950

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • catalyses the post-translocational folding of exported proteins PubMed, required for folding of penicillin-binding proteins (PbpA, PbpB, PbpC, PbpD) PubMed

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

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • PrsA is a lipoprotein with a N-acetyl-S-diacyl-glyceryl-cysteine structure PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • dimeric or oligomeric protein PubMed

• Localization:
  • membrane associated (lipoprotein) PubMed
  • distinct spots organized in a helical pattern along the cell membrane PubMed

Database entries

• Structure: 1ZK6

• UniProt: P24327

• KEGG entry: [2]

• E.C. number: 5.2.1.8

Expression and regulation

• Operon: prsA PubMed

• Expression browser: prsA PubMed

• Sigma factor:

• 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:

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)