CH60_PARTM
ID CH60_PARTM Reviewed; 539 AA.
AC Q8VV84;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
OS Parageobacillus thermoglucosidasius (Geobacillus thermoglucosidasius).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX NCBI_TaxID=1426;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43742 / DSM 2542 / NCIMB 11955 / NRRL B-14516 / KP 1006;
RX PubMed=11834128; DOI=10.1042/ba20010064;
RA Watanabe K., Fujiwara H., Inui K., Suzuki Y.;
RT "Oligo-1,6-glucosidase from a thermophile, Bacillus thermoglucosidasius
RT KP1006, was efficiently produced by combinatorial expression of GroEL in
RT Escherichia coli.";
RL Biotechnol. Appl. Biochem. 35:35-43(2002).
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; AB025944; BAB83940.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VV84; -.
DR SMR; Q8VV84; -.
DR STRING; 1426.AOT13_04590; -.
DR eggNOG; COG0459; Bacteria.
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..539
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063281"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 86..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 476..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 539 AA; 57193 MW; 7C6BE183F07C67B5 CRC64;
MAKEIKFSEE ARRAMLRGVD KLADAVKVTL GPKGRNVVLE KKFGSPLITN DGVTIAKEIE
LEDPFENMGA KLVAEVASKT NDVAGDGTTT ATVLAQAMIR EGLKNVTAGA NPMGIRKGIE
KAVAVAVEEL KAISKPIQGK ESIAQVAAIS AADEEVGQLI AEAMERVGND GVITLEESKG
FTTELDVVEG MQFDRGYASP YMITDTEKME AVLENPYILI TDKKISNIQD ILPILEQVVQ
QGKPLLIIAE DVEGEALATL VVNKLRGTFT AVAVKAPGFG DRRKAMLEDI AILTGGEVIS
EELGRELKST TIASLGRASK VVVTKENTTI VEGAGDSERI KARINQIRAQ LEETTSEFDR
GKLQERLAKL AGGVAVIKVG AATETELKER KLRIEDALNS TRAAVEEGIV AGGGTALMNV
YNKVAAIEAE GDEATGVKIV LRAIEEPVRQ IAQNAGLEGS VIVERLKSEK PGIGFNAATG
EWVNMIEAGI VDPTKVTRSA LQNAASVAAM FLTTEAVVAD KPEENKGGNS GMPDMGGMM
