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]Gene
Coordinates
1,070,364 1,071,242
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|3B4F035535D6504405567E7C44E72902A11F7447|PbpA], [protein|EBEFF9E0A524DCDA19382E5401B923B805E4C559|PbpB], [protein|5BBA2769A9C0EDB56625F008A55470C2E2885AA4|PbpC], [protein|E50D4B30C2A0987A356C988AF8A4951C0CDF6C06|PbpD]) [Pubmed|20487272][protein]-peptidylproline (ω=180) --> [protein]-peptidylproline (ω=0) (according to UniProt)Protein family
PrsA family (single member, according to UniProt)[SW|Domains]
PpiC domain (aa 134-224) (according to UniProt)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]Expression and Regulation
Operons
genes
[gene|6EE13E61A218A6D52BAC83A1145B0B96961CE289|prsA]
description
[Pubmed|22383849]
additional information
[protein|search|PrsA] is subject to degradation by [protein|search|WprA] and other extracellular proteases [PubMed|24362423]view in new tabReferences
Reviews
Original publications
12634326,14976191,11807061,10096076,18763711,10871614,20487272,22303020,24362423,25525259,31254548,31530286