U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

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

    Gene ID: 948726, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    fklB
    Official Full Name
    peptidyl-prolyl cis-trans isomerase FklB
    Primary source
    ECOCYC:G7865
    Locus tag
    b4207
    See related
    ASAP:ABE-0013759
    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
    ECK4203; ytfC
    Summary
    Binds TrxA (Kumar, 2004). [More information is available at EcoGene: EG12503]. The FklB protein is a periplasmic FKBP-type peptidyl-prolyl cis/trans-isomerase . [More information is available at EcoCyc: G7865].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (4428935..4429555)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF2686 domain-containing protein YjfZ Neighboring gene pseudo Neighboring gene cell division protein YtfB Neighboring gene D-serine/alanine/glycine/:H(+)symporter Neighboring gene iron-sulfur cluster repair protein YtfE

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. The helix located between the two domains of a mip-like peptidyl-prolyl cis-trans isomerase is crucial for its structure, stability, and protein folding ability. Jana B, et al. Biochemistry, 2012 Oct 9. PMID 22989269
    2. Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli. Kumar JK, et al. Proc Natl Acad Sci U S A, 2004 Mar 16. PMID 15004283, Free PMC Article
    3. From the genome sequence to the proteome and back: evaluation of E. coli genome annotation with a 2-D gel-based proteomics approach. Maillet I, et al. Proteomics, 2007 Apr. PMID 17366475
    4. Isolation and amino acid sequence of a new 22-kDa FKBP-like peptidyl-prolyl cis/trans-isomerase of Escherichia coli. Similarity to Mip-like proteins of pathogenic bacteria. Rahfeld JU, et al. J Biol Chem, 1996 Sep 6. PMID 8703024
    5. Global analysis of candidate genes important for fitness in a competitive biofilm using DNA-array-based transposon mapping. Junker LM, et al. Microbiology (Reading), 2006 Aug. PMID 16849790

    See all (14) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on mature peptide
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    Submit: New GeneRIF Correction

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables FK506 binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables peptidyl-prolyl cis-trans isomerase activity IBA
    Inferred from Biological aspect of Ancestor
    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 homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    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 HDA PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    peptidyl-prolyl cis-trans isomerase FklB
    NP_418628.4

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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
      4428935..4429555
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418628.4 peptidyl-prolyl cis-trans isomerase FklB [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418628.4

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2X1MKC5
      Conserved Domains (1) summary
      PRK11570
      Location:1 → 206
      PRK11570; peptidyl-prolyl cis-trans isomerase; Provisional
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.