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: PrsA
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
• the mutant is viable in the presence of elevated concentrations of Mg²⁺ PubMed

Database entries

• BsubCyc: BSU09950

• 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

• BsubCyc: BSU09950

• 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
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1845 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 5530 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Zhen Kang, Sen Yang, Guocheng Du, Jian Chen
Molecular engineering of secretory machinery components for high-level secretion of proteins in Bacillus species.
J Ind Microbiol Biotechnol: 2014, 41(11);1599-607
[PubMed:25212246] [WorldCat.org] [DOI] (I p)