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

Gene ID: 944812, updated on 23-Sep-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. Conformational Dynamics of the Periplasmic Chaperone SurA. Jia M, et al. Biochemistry, 2020 Sep 8. PMID 32786408
  3. Domain interactions determine the conformational ensemble of the periplasmic chaperone SurA. Marx DC, et al. Protein Sci, 2020 Oct. PMID 32748422, Free PMC Article
  4. The Role of SurA PPIase Domains in Preventing Aggregation of the Outer-Membrane Proteins tOmpA and OmpT. Humes JR, et al. J Mol Biol, 2019 Mar 15. PMID 30716334
  5. The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain. Soltes GR, et al. J Bacteriol, 2016 Jan 4. PMID 26728192, Free PMC Article

See all (82) 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 peptide binding 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 
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 
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 
Component Evidence Code Pubs
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
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