lipoprotein, post-translocational folding of exported proteins (post-translocation molecular chaperone)
product
post-translocation molecular chaperone
Genomic Context
categories
[category|SW 3|Information processing] → [category|SW 3.3|Protein synthesis, modification and degradation] → [category|SW 3.3.5|Protein secretion][category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes][category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins][SW|Categories] containing this gene/protein
[SW|protein secretion], [SW|essential genes], [SW|membrane proteins]Gene
Phenotypes of a mutant
essential [Pubmed|20487272,12682299]the mutant is viable in the presence of elevated concentrations of Mg2+ [Pubmed|20487272]The protein
Catalyzed reaction/ biological activity
catalyses the post-translocational folding of exported proteins [Pubmed|20487272], required for folding of [[penicillin-binding proteins]] ([protein|search|PbpA], [protein|search|PbpB], [protein|search|PbpC], [protein|search|PbpD]) [Pubmed|20487272]Protein family
PpiC domain (according to Swiss-Prot)Modification
PrsA is a lipoprotein with a N-acetyl-S-diacyl-glyceryl-cysteine structure [Pubmed|22303020]Structure
[PDB|1ZK6][SW|Localization]
membrane associated (lipoprotein) [Pubmed|22303020]distinct spots organized in a helical pattern along the cell membrane [Pubmed|20487272][SW|Interactions]
dimeric or oligomeric protein [Pubmed|20487272]Expression and Regulation
Operon
''[protein|search|prsA]'' [Pubmed|22383849]References
Reviews
Original publications
12634326,14976191,11807061,10096076,18763711,10871614,20487272,22303020,24362423,25525259 
