CH60_TETHA
ID CH60_TETHA Reviewed; 546 AA.
AC Q93GT6;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 87.
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 Tetragenococcus halophilus (Pediococcus halophilus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Tetragenococcus.
OX NCBI_TaxID=51669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12092841; DOI=10.1271/bbb.66.1176;
RA Fukuda D., Watanabe M., Aso Y., Sonomoto K., Ishizaki A.;
RT "The groESL operon of the halophilic lactic acid bacterium Tetragenococcus
RT halophila.";
RL Biosci. Biotechnol. Biochem. 66:1176-1180(2002).
RN [2]
RP SEQUENCE REVISION TO 100-103; 281; 387-389 AND C-TERMINUS.
RA Nakayama J., Fukuda D., Watanabe M., Aso Y., Sonomoto K., Ishizaki A.;
RL Submitted (JUL-2004) 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; AB073399; BAB70661.2; -; Genomic_DNA.
DR PIR; JC7858; JC7858.
DR AlphaFoldDB; Q93GT6; -.
DR SMR; Q93GT6; -.
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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT CHAIN 1..546
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063577"
FT REGION 521..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 546 AA; 57804 MW; 9284CE1B9743FC75 CRC64;
MAKDIKFSED ARRSMLNGVS KLADTVKVTL GPRGRNVVLE KSYGSPLITN DGVTIAKEIE
LENRFENMGA QLVSEVASKT NDIAGDGTTT ATVLAQSIVS EGLKNVTSGA NPLGIRRGIE
QATQKAVEEL QNISTPVESK EAIVQVGEVS SGSKQVGQYI ADAMDKVGND GVITIEDSQG
IDTELDVVEG MQFDRGYLSQ YMVTDNEKME ADLDSPYILI TDKKISNIQD ILPLLEQVVQ
ESKPLLIIAD DIDGEALPTL VLNKIRGTFN VVATKAPGFG DRRKAMLEDI AVLTGATVIT
EDLGLELKDA TMDSLGKANK VTVDKDNTTI VEGAGDSTAI EDRVQLIKNQ VAETTSDFDR
EKLQERLAKL AGGVAVIKVG AATETEQKEL KLRIEDALNA ARAGVEEGMV SGGGTALVNV
INKVAELDAD DDAITGVNIV LRALEEPVRQ ISENAGFEGS VIIEKLKSEK LGIGFNAATG
QWVNMVDAGI VDPTKVVRSA LQNAASISAL LLSTEAVIAD RPDESGNDAG AGAQGMDPSM
MGGGMM
