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    groL chaperonin GroEL [ Prochlorococcus marinus str. MIT 9515 ]

    Gene ID: 60201397, updated on 31-Mar-2024

    Summary

    Gene symbol
    groL
    Gene description
    chaperonin GroEL
    Locus tag
    P9515_RS07695
    Gene type
    protein coding
    Organism
    Prochlorococcus marinus str. MIT 9515 (strain: MIT 9515)
    Lineage
    Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Prochlorococcaceae; Prochlorococcus
    Old locus tag
    P9515_16151
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    Genomic context

    Sequence:
    NC_008817.1 (1411077..1412711, complement)

    NC_008817.1Genomic Context describing neighboring genes Neighboring gene 2,3-bisphosphoglycerate-independent phosphoglycerate mutase Neighboring gene preprotein translocase subunit SecG Neighboring gene co-chaperone GroES Neighboring gene F0F1 ATP synthase subunit beta

    General protein information

    Preferred Names
    chaperonin GroEL
    WP_011820917.1
    • 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds

    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_008817.1 Reference assembly

      Range
      1411077..1412711 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. WP_011820917.1 chaperonin GroEL [Prochlorococcus marinus]

      See identical proteins and their annotated locations for WP_011820917.1

      UniProtKB/Swiss-Prot
      A2BYG1
      UniProtKB/TrEMBL
      A0A9D9G0Y9
      Conserved Domains (2) summary
      PRK12850
      Location:1540
      groEL; chaperonin GroEL; Reviewed
      cl02777
      Location:1528
      chaperonin_like; chaperonin_like superfamily. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. There are 2 main chaperonin groups. The symmetry of type I ...