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    surA chaperone SurA [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944812, updated on 3-Dec-2024

    Summary

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    Official Symbol
    surA
    Official Full Name
    chaperone SurA
    Primary source
    ECOCYC:EG10985
    Locus tag
    b0053
    See related
    ASAP:ABE-0000180
    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
    ECK0054
    Summary
    Parvulin (ppiC) family. [More information is available at EcoGene: EG10985]. SurA in Escherichia coli is a periplasmic peptidyl-prolyl isomerase which is necessary for the proper folding of outer membrane proteins including OmpA, OmpF and LamB. [More information is available at EcoCyc: EG10985].
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    Genomic context

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    Sequence:
    NC_000913.3 (53416..54702, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF525 domain-containing protein ApaG Neighboring gene 16S rRNA m(6)2A1518,m(6)2A1519 dimethyltransferase Neighboring gene 4-hydroxythreonine-4-phosphate dehydrogenase Neighboring gene lipopolysaccharide assembly protein LptD Neighboring gene co-chaperone protein DjlA

    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. Interaction of the periplasmic chaperone SurA with the inner membrane protein secretion (SEC) machinery. Troman LA, et al. Biochem J, 2023 Feb 27. PMID 36701201, Free PMC Article
    2. SurA assists the folding of Escherichia coli outer membrane proteins. Lazar SW, et al. J Bacteriol, 1996 Mar. PMID 8626309, Free PMC Article
    3. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. Behrens S, et al. EMBO J, 2001 Jan 15. PMID 11226178, Free PMC Article
    4. Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id essential and sufficient for peptide binding. Webb HM, et al. J Biol Chem, 2001 Dec 7. PMID 11546789
    5. Periplasmic chaperones--new structural and functional insights. Behrens S. Structure, 2002 Nov. PMID 12429086

    See all (83) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Dual client binding sites in the ATP-independent chaperone SurA.
      Title: Dual client binding sites in the ATP-independent chaperone SurA.
    2. Interaction of the periplasmic chaperone SurA with the inner membrane protein secretion (SEC) machinery.
      Title: Interaction of the periplasmic chaperone SurA with the inner membrane protein secretion (SEC) machinery.
    3. The transmembrane supercomplex mediating the biogenesis of OMPs in Gram-negative bacteria assumes a circular conformational change upon activation.
      Title: The transmembrane supercomplex mediating the biogenesis of OMPs in Gram-negative bacteria assumes a circular conformational change upon activation.
    4. Conformational Dynamics of the Periplasmic Chaperone SurA.
      Title: Conformational Dynamics of the Periplasmic Chaperone SurA.
    5. Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA.
      Title: Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA.
    6. The core domain of SurA endows its generic chaperone ability, while the presence of PPIase domains enhances its chaperone activity for specific OMPs, suggesting one reason for the conservation of multiple PPIase domains in SurA in proteobacteria.
      Title: The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT.
    7. Skp can dissolve aggregated OmpC while SurA cannot convert aggregated OmpC into the monodisperse form and the conformations of OmpC recognized by the two chaperones as well as their stoichiometries of binding are different.
      Title: Single-Molecule Detection Reveals Different Roles of Skp and SurA as Chaperones.
    8. SurA cycles between distinct conformational and functional states during the bacterial outer membrane assembly process.
      Title: The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain.
    9. These findings suggest an autoinhibitory mechanism for regulation of SurA chaperone activity through interdomain interactions involving a proline isomerase domain.
      Title: The activity and specificity of the outer membrane protein chaperone SurA are modulated by a proline isomerase domain.
    10. mutational studies on SurA to identify residues that are critical for function were conducted; formation of disulfide bond in mutants has no observable detrimental effect on protein activity, indicating SurA does not undergo large-scale conformational change while performing its function
      Title: Insights into the function and structural flexibility of the periplasmic molecular chaperone SurA.
    Submit: New GeneRIF Correction See all GeneRIFs (19)

    General gene information

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    Homology

    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 peptide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables unfolded protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables unfolded protein binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables unfolded protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in Gram-negative-bacterium-type cell outer membrane assembly IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within Gram-negative-bacterium-type cell outer membrane assembly IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    acts_upstream_of_or_within Gram-negative-bacterium-type cell outer membrane assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in chaperone-mediated protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within maintenance of stationary phase IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within maintenance of unfolded protein IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein folding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein stabilization IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein stabilization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein stabilization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in regulation of transcription by RNA polymerase II IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in outer membrane-bounded periplasmic space IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in outer membrane-bounded periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    chaperone SurA
    NP_414595.1

    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
      53416..54702 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414595.1 chaperone SurA [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414595.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7EDZ1
      Conserved Domains (1) summary
      PRK10770
      Location:19 → 428
      PRK10770; peptidyl-prolyl cis-trans isomerase SurA; Provisional
    Nucleotide Protein
    Heading Accession and Version

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