prsA
168
lipoprotein, post-translocational folding of exported proteins (post-translocation molecular chaperone)
locus
BSU_09950
Molecular weight
32.36 kDa
pI
9.12
function
protein folding
product
post-translocation molecular chaperone
essential
yes
ec
5.2.1.8
synonyms
prsA
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG0760 (Galperin et al., 2021)
This gene is a member of the following regulons
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)
[wiki|Domains]
PpiC domain (aa 134-224) (according to UniProt)
Structure
[PDB|1ZK6]
[AF|P24327]
Modification
PrsA is a lipoprotein with a N-acetyl-S-diacyl-glyceryl-cysteine structure [Pubmed|22303020]
[wiki|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]
References
Reviews
Original Publications
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Time of last update: 2024-10-12 19:47:10
Author of last update: Jstuelk