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

Summary

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Official Symbol: ppiB
Official Full Name: peptidyl-prolyl cis-trans isomerase B
Primary source: ECOCYC:EG10758
Locus tag: b0525
See related: ASAP:ABE-0001806
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_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

1.3 A Crystal Structure of E. coli Peptidyl-Prolyl Isomerase B with Uniform Substitution of Valine by (2S,3S)-4-Fluorovaline Reveals Structure Conservation and Multiple Staggered Rotamers of CH2F Groups.
Title: 1.3 Å Crystal Structure of E. coli Peptidyl-Prolyl Isomerase B with Uniform Substitution of Valine by (2S,3S)-4-Fluorovaline Reveals Structure Conservation and Multiple Staggered Rotamers of CH(2)F Groups.
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.
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.
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.
N-terminus verified by Edman degradation on complete protein
Title: '98 Escherichia coli SWISS-2DPAGE database update.

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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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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables RNA polymerase II CTD heptapeptide repeat P3 isomerase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat P6 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
involved_in regulation of transcription by RNA polymerase II	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

EC 5.2.1.8

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

NC_000913.3 Reference assembly

Range

553943..554437 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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

A0A5B9AKW5

Conserved Domains (1) summary

PRK10791
Location:1 → 164

PRK10791; peptidylprolyl isomerase B