MULTISPECIES: chaperonin GroEL [Listeria].

LOCUS       WP_003726503             542 aa            linear   BCT 23-JUN-2024
ACCESSION   WP_003726503
VERSION     WP_003726503.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 542)
  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..542
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     gene            1..542
                     /gene="groL"
     Protein         1..542
                     /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=57237
     Region          1..531
                     /region_name="groEL"
                     /note="chaperonin GroEL; Reviewed; PRK00013"
                     /db_xref="CDD:234573"
     Site            order(3,7,24,35..38,40,45..46,48,58,60,68,72,75,195,227,
                     255,382,384,456,510,513..519)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239460"
     Site            order(30..32,86,90,149,396,413,451,490,492)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239460"
     Site            order(108,431,449,458,460..461,464)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239460"
     Site            order(140,184,191,373,407..408)
                     /site_type="other"
                     /note="hinge regions"
                     /db_xref="CDD:239460"
ORIGIN      
        1 makdikfsed arramlrgvd qlanavkvtl gpkgrnvvle kkfgsplitn dgvtiakeie
       61 ledpfenmga klvsevaskt ndvagdgttt atvlaqamiq eglknvtaga npvgvrrgie
      121 kavataieel kaiskpiesk esiaqvaais sgdeevgkli aeamervgnd gvitieeskg
      181 fateldvveg mqfdrgytsp ymvtdsdkme avlekpyili tdkkinniqe ilpvleqvvq
      241 qgrpmliiae dvegeaqatl vlnklrgtfn vvavkapgfg drrkamledi ailtggqvit
      301 edlglelkta tvdqlgtank vvvtkddtti vegagdstqi sarvnqiraq meettsefdr
      361 eklqerlakl aggvavvkvg aatetelker klriedalns traaveegiv agggtalvsi
      421 ynkvaaleae gdvetginiv lrsleepvrq iahnaglegs viverlkhea vgvgfnaang
      481 ewvnmidagi vdptkvtrsa lqnassvaal lltteavvad kpdengpaav pdmgmggmgg
      541 mm