CH60_THEBR
ID CH60_THEBR Reviewed; 541 AA.
AC Q60024;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
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;
OS Thermoanaerobacter brockii (Thermoanaerobium brockii).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=29323;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RT8.G4;
RX PubMed=9795109; DOI=10.1016/s0378-1119(98)00382-5;
RA Truscott K.N., Scopes R.K.;
RT "Sequence analysis and heterologous expression of the groE genes from
RT Thermoanaerobacter sp. Rt8.G4.";
RL Gene 217:15-23(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-44, CHARACTERIZATION, AND MASS SPECTROMETRY.
RC STRAIN=RT8.G4;
RX PubMed=7912671; DOI=10.1111/j.1432-1033.1994.tb18866.x;
RA Truscott K.N., Hoej P.B., Scopes R.K.;
RT "Purification and characterization of chaperonin 60 and chaperonin 10 from
RT the anaerobic thermophile Thermoanaerobacter brockii.";
RL Eur. J. Biochem. 222:277-284(1994).
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 -!- MASS SPECTROMETRY: Mass=57949; Mass_error=10; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7912671};
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; U56021; AAB00559.1; -; Genomic_DNA.
DR PIR; S72614; S72614.
DR AlphaFoldDB; Q60024; -.
DR SMR; Q60024; -.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7912671"
FT CHAIN 2..541
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063578"
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 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 44
FT /note="G -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 58060 MW; 6C3316AD289B352B CRC64;
MAKQIKYGEE ARRALERGVN AVADTVKVTL GPRGRNVVLD KKYGSPTVTN DGVTIAREIE
LEDPFENQGA QLLKEAATKT NDIAGDGTTT ATLLAQAMVR EGLKNLAAGA NPMLLRRGIA
KAVDAAVEGL KRISKPIDNK ESIAHVASIS AADEEIGKLI AEAMDKVGKD GVITVEESKT
LGTTLEVVEG MQFDRGYISP YMVTDAEKME AVLEEPVILI TDKKISNIQD LLPLLEQIVQ
QGKKLLIIAD DVEGEALATL IVNKLRGTFT CVAVKAPGFG DRRKEMLQDI AILTGGQVIS
EELGYDLKDV RLDMLGRARQ VKVTKEYTTI VGGAGDPSEI KKRVNQIKAQ IEETTSDYDR
EKLQERLAKL AGGVAVIQAG AATETELKEK KHRIEDALAA TKAAVEEGIV PGGGIALLNV
IEDVQKVVDS LEGDFKTGAK IVLRALEEPV RQIATNAGVD GSVIVEKIKA AKDPNFGYDA
YKEEFTDMFK AGIVDPTKVT RTALQNAASI ASMILTTEAI VVDIPEKNTG MPNPGAGMDM
M
