CH60_BUCMP
ID CH60_BUCMP Reviewed; 548 AA.
AC O51832; Q93T48;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA, symL;
OS Buchnera aphidicola subsp. Myzus persicae (Myzus persicae primary
OS endosymbiont).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=98795;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9420234; DOI=10.1128/jvi.72.1.358-365.1998;
RA Hogenhout S.A., van der Wilk F., Verbeek M., Goldbach R.W.,
RA van den Heuvel J.F.J.M.;
RT "Potato leafroll virus binds to the equatorial domain of the aphid
RT endosymbiotic GroEL homolog.";
RL J. Virol. 72:358-365(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cui X., Wu Y., Lin L.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential
CC role in assisting protein folding. The GroEL-GroES system forms a nano-
CC cage that allows encapsulation of the non-native substrate proteins and
CC provides a physical environment optimized to promote and accelerate
CC protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00600};
CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC rings stacked back-to-back. Interacts with the co-chaperonin GroES.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; AF003957; AAC04237.1; -; Genomic_DNA.
DR EMBL; AF367248; AAK52957.1; -; Genomic_DNA.
DR AlphaFoldDB; O51832; -.
DR SMR; O51832; -.
DR PRIDE; O51832; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT CHAIN 1..548
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063309"
FT REGION 524..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 87..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 479..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 111
FT /note="M -> K (in Ref. 2; AAK52957)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="V -> M (in Ref. 2; AAK52957)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="Q -> H (in Ref. 2; AAK52957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 57883 MW; AD61917965E4184A CRC64;
MAAKDVKFGN EARIKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPSIT KDGVSVAREI
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATLLAQSIV NEGLKAVAAG MNPMDLKRGI
DKAVISAVEE LKNLSVPCSD SKAITQVGTI SANADEKVGA LIAEAMEKVG NDGVITVEEG
TGLQNELEVV KGMQFDRGYL SPYFINKPET GIVELENPYI LVADKKISNV REMLPILESV
AKSGKPLLII SEDLEGEALA TLVVNSMRGI VKVAAVKAPG FGDRRKAMLQ DISILTGGSV
ISEELAMELE KSTLEDLGQA KRVVISKDTT TIIGGVGEKH TIQSRISQIR QEIQEATSDY
DKEKLNERLA KLSGGVAVLK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALV
RVAGKTSNLR GQNEDQNVGI RVALRAMEAP LRQIVSNSGE EPSVVTNNVK DGKGNYGYNA
ATDEYGDMID FGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKEDKS SDSNSSPAGG
MGGMGGMM
