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prsA molecular chaperone lipoprotein [ Bacillus subtilis subsp. subtilis str. 168 ]

Gene ID: 939294, updated on 12-Feb-2021
Gene symbol
prsA
Gene description
molecular chaperone lipoprotein
Locus tag
BSU_09950
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bacillus subtilis subsp. subtilis str. 168 (strain: 168, sub-species: subtilis, type-material: type strain of Bacillus subtilis)
Lineage
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus
Old locus tag
BSU09950
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Sequence:
NC_000964.3 (1070364..1071242, complement)

NC_000964.3Genomic Context describing neighboring genes Neighboring gene 3'-5' exonuclease Neighboring gene sporulation factor Neighboring gene spore assembly and germination protein Neighboring gene spore and germination protein

Genomic Sequence:
NC_000964.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis. Hyyryläinen HL, et al. Mol Microbiol, 2010 Jul 1. PMID 20487272
  2. NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis. Tossavainen H, et al. FEBS Lett, 2006 Mar 20. PMID 16516208
  3. Bacillus subtilis, the model Gram-positive bacterium: 20 years of annotation refinement. Borriss R, et al. Microb Biotechnol, 2018 Jan. PMID 29280348, Free PMC Article
  4. An updated metabolic view of the Bacillus subtilis 168 genome. Belda E, et al. Microbiology (Reading), 2013 Apr. PMID 23429746
  5. From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later. Barbe V, et al. Microbiology (Reading), 2009 Jun. PMID 19383706, Free PMC Article

See all (6) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Misfolded PBP2a was detected in PrsA-depleted cells, indicating that PrsA is required for the folding of this penicillin binding protein either directly or indirectly.
    Title: Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis.
  2. the NMR solution structure of the PPIase domain of PrsA
    Title: NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis.
Submit: New GeneRIF Correction

Homology

Preferred Names
molecular chaperone lipoprotein
NP_388876.1
  • Evidence 1a: Function from experimental evidences in the studied strain; PubMedId: 12634326, 12682299, 14976191, 16516208, 25525259, 26711778; Product type lp : lipoprotein

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000964.3 Reference assembly

    Range
    1070364..1071242 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_388876.1 molecular chaperone lipoprotein [Bacillus subtilis subsp. subtilis str. 168]

    See identical proteins and their annotated locations for NP_388876.1

    Status: PROVISIONAL

    Conserved Domains (1) summary
    PRK04405
    Location:1 → 273
    prsA; peptidylprolyl isomerase; Provisional
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P24327.1

Gene LinkOut

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Other Literature Sources
Molecular Biology Databases
Research Materials