CH60_THETH
ID CH60_THETH Reviewed; 145 AA.
AC P61491; P45746; Q60018; Q9RA44;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 73.
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};
DE AltName: Full=Heat shock protein 60;
DE Flags: Fragment;
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=cpnL, groL {ECO:0000255|HAMAP-Rule:MF_00600}, hsp60, mopA;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=10329779; DOI=10.1107/s0907444999003698;
RA Walsh M.A., Dementieva I., Evans G., Sanishvili R., Joachimiak A.;
RT "Taking MAD to the extreme: ultrafast protein structure determination.";
RL Acta Crystallogr. D 55:1168-1173(1999).
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, ECO:0000305}.
CC -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC 1SRV. {ECO:0000305}.
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DR PDB; 1SRV; X-ray; 1.70 A; A=1-145.
DR PDBsum; 1SRV; -.
DR AlphaFoldDB; P61491; -.
DR SMR; P61491; -.
DR EvolutionaryTrace; P61491; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Isomerase;
KW Nucleotide-binding.
FT CHAIN <1..>145
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063583"
FT NON_TER 1
FT NON_TER 145
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1SRV"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1SRV"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:1SRV"
FT STRAND 21..36
FT /evidence="ECO:0007829|PDB:1SRV"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:1SRV"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:1SRV"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1SRV"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1SRV"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:1SRV"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:1SRV"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1SRV"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1SRV"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1SRV"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1SRV"
SQ SEQUENCE 145 AA; 15736 MW; 7E02F2AE0DF7C024 CRC64;
GYQFDKGYIS PYFVTNPETM EAVLEDAFIL IVEKKVSNVR ELLPILEQVA QTGKPLLIIA
EDVEGEALAT LVVNKLRGTL SVAAVKAPGF GDRRKEMLKD IAAVTGGTVI SEELGFKLEN
ATLSMLGRAE RVRITKDETT IVGGK
