MULTISPECIES: chaperonin GroEL [Pseudomonas].

LOCUS       WP_003094059             547 aa            linear   BCT 23-JUN-2024
ACCESSION   WP_003094059
VERSION     WP_003094059.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 547)
  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..547
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..547
                     /gene="groL"
     Protein         1..547
                     /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=56955
     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 maakevkfgd sarkkmlvgv nvladavkat lgpkgrnvvl dksfgaptit kdgvsvakei
       61 elkdkfenmg aqlvkdvask andaagdgtt tatvlaqaiv neglkavaag mnpmdlkrgi
      121 dkatvaivaq lkelakpcad tkaiaqvgti sansdesigq iiaeamekvg kegvitveeg
      181 sglenelsvv egmqfdrgyl spyfvnkpdt maaeldspll llvdkkisni remlpvleav
      241 akagrplliv aedvegeala tlvvnnmrgi vkvaavkapg fgdrrkamlq diailtggtv
      301 iseevglsle gatlehlgna krvvinkent tiidgagvqa diearvlqir kqieettsdy
      361 dreklqerla klaggvavik vgaatevemk ekkarvedal hatraaveeg vvpgggvalv
      421 ralqaieglk gdneeqnvgi allrravesp lrqivanagd epsvvvdkvk qgsgnygfna
      481 atgvygdmie mgildpakvt rsalqaaasi gglmitteam vaeivedkpa mggmpdmggm
      541 ggmggmm