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ppiB peptidyl-prolyl cis-trans isomerase B [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 949038, updated on 4-Apr-2024

Summary

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Gene symbol
ppiB
Gene description
peptidyl-prolyl cis-trans isomerase B
Primary source
ASAP:ABE-0001806
Locus tag
b0525
See related
ECOCYC:EG10758
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0518
Summary
PpiB is down 6X during growth at 4C (enabled by Oleispira antarctica Cpn10/60 transgene). [More information is available at EcoGene: EG10758]. PpiB is a peptidyl-prolyl cis-trans-isomerase (PPIase), catalyzing the conformational isomerization of prolyl residues in peptides. [More information is available at EcoCyc: EG10758].
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Genomic context

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Sequence:
NC_000913.3 (553943..554437, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene 5-(carboxyamino)imidazole ribonucleotide synthase Neighboring gene N(5)-carboxyaminoimidazole ribonucleotide mutase Neighboring gene UDP-2,3-diacylglucosamine diphosphatase Neighboring gene cysteine--tRNA ligase Neighboring gene PF04307 family inner membrane protein YbcI

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Functional analysis of the cyclophilin PpiB role in bacterial cell division. Skagia A, et al. Genes Cells, 2017 Sep. PMID 28752912
  2. Structural and functional analysis of cyclophilin PpiB mutants supports an in vivo function not limited to prolyl isomerization activity. Skagia A, et al. Genes Cells, 2017 Jan. PMID 27868330
  3. Fast folding of Escherichia coli cyclophilin A: a hypothesis of a unique hydrophobic core with a phenylalanine cluster. Ikura T, et al. J Mol Biol, 2000 Mar 31. PMID 10731429
  4. Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation. Edwards KJ, et al. J Mol Biol, 1997 Aug 15. PMID 9268657
  5. Identification of Substrates of Cytoplasmic Peptidyl-Prolyl Cis/Trans Isomerases and Their Collective Essentiality in Escherichia Coli. Klein G, et al. Int J Mol Sci, 2020 Jun 13. PMID 32545723, Free PMC Article

See all (27) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. PpiB is able to control bacterial cell division by modulating early divisome components zipA and ftsZ.
    Title: Functional analysis of the cyclophilin PpiB role in bacterial cell division.
  2. The combination of enzymatic studies concerning the PPIase and chaperone activities of each mutant protein, with structural analyses based on 3D models, provided further insights into the effects of the mutations on the function of PpiB and showed the importance of structural features in addition to the catalytic site, for its in vivo role.
    Title: Structural and functional analysis of cyclophilin PpiB mutants supports an in vivo function not limited to prolyl isomerization activity.
  3. For DnaK, acetyl-CoA carboxylase, biotin carboxylase subunit (AccC) and phosphate acetyltransferase (Pta) we also showed a direct role of PpiB in the functional control of these proteins because it increased the measured enzyme activity of each protein and further interfered with DnaK localization and the correct folding of AccC.
    Title: Cyclophilin PpiB is involved in motility and biofilm formation via its functional association with certain proteins.
  4. N-terminus verified by Edman degradation on complete protein
    Title: '98 Escherichia coli SWISS-2DPAGE database update.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables isomerase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidyl-prolyl cis-trans isomerase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptidyl-prolyl cis-trans isomerase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within chaperone-mediated protein folding IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within chaperone-mediated protein folding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
peptidyl-prolyl cis-trans isomerase B
NP_415058.1

NCBI Reference Sequences (RefSeq)

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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_000913.3 Reference assembly

    Range
    553943..554437 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415058.1 peptidyl-prolyl cis-trans isomerase B [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415058.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A5B9AA66, A0A827QMP8
    Conserved Domains (1) summary
    PRK10791
    Location:1 → 164
    PRK10791; peptidylprolyl isomerase B
Nucleotide Protein
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