MULTISPECIES: chaperonin GroEL [Enterobacteriaceae].

LOCUS       WP_000729117             548 aa            linear   BCT 23-JUN-2024
ACCESSION   WP_000729117
VERSION     WP_000729117.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Walter,S.
  TITLE     Structure and function of the GroE chaperone
  JOURNAL   Cell Mol Life Sci 59 (10), 1589-1597 (2002)
   PUBMED   12475168
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR02348.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..548
                     /gene="groL"
     Protein         1..548
                     /product="chaperonin GroEL"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /GO_process="GO:0042026 - protein refolding [Evidence
                     IEA]"
                     /note="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; 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"
                     /calculated_mol_wt=57198
     Region          2..530
                     /region_name="groEL"
                     /note="chaperonin GroEL; Reviewed; PRK00013"
                     /db_xref="CDD:234573"
     Site            order(4,8,25,36..39,41,46..47,49,59,61,69,73,76,197,229,
                     257,384,386,459,513,516..522)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239460"
     Site            order(31..33,87,91,150,398,415,454,493,495)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239460"
     Site            order(109,434,452,461,463..464,467)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239460"
     Site            order(141,186,193,375,409..410)
                     /site_type="other"
                     /note="hinge regions"
                     /db_xref="CDD:239460"
ORIGIN      
        1 maakdvkfgn darvkmlrgv nvladavkvt lgpkgrnvvl dksfgaptit kdgvsvarei
       61 eledkfenmg aqmvkevask andaagdgtt tatvlaqaii teglkavaag mnpmdlkrgi
      121 dkavtaavee lkalsvpcsd skaiaqvgti sansdetvgk liaeamdkvg kegvitvedg
      181 tglqdeldvv egmqfdrgyl spyfinkpet gavelespfi lladkkisni remlpvleav
      241 akagkpllii aedvegeala tlvvntmrgi vkvaavkapg fgdrrkamlq diatltggtv
      301 iseeigmele katledlgqa krvvinkdtt tiidgvgeea aiqgrvaqir qqieeatsdy
      361 dreklqerva klaggvavik vgaatevemk ekkarvedal hatraaveeg vvagggvali
      421 rvaskladlr gqnedqnvgi kvalrameap lrqivlncge epsvvantvk ggdgnygyna
      481 ateeygnmid mgildptkvt rsalqyaasv aglmittecm vtdlpkndaa dlgaaggmgg
      541 mggmggmm