CH60_CLOPE
ID CH60_CLOPE Reviewed; 539 AA.
AC P26821;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 130.
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;
GN OrderedLocusNames=CPE2289;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1347462; DOI=10.1016/0167-4781(92)90468-f;
RA Rusanganwa E., Singh B., Gupta R.S.;
RT "Cloning of HSP60 (GroEL) operon from Clostridium perfringens using a
RT polymerase chain reaction based approach.";
RL Biochim. Biophys. Acta 1130:90-94(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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; X62914; CAA44697.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB81995.1; -; Genomic_DNA.
DR PIR; S22342; S22342.
DR RefSeq; WP_003462314.1; NC_003366.1.
DR AlphaFoldDB; P26821; -.
DR SMR; P26821; -.
DR STRING; 195102.gene:10491597; -.
DR EnsemblBacteria; BAB81995; BAB81995; BAB81995.
DR KEGG; cpe:CPE2289; -.
DR HOGENOM; CLU_016503_6_1_9; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000000818; Chromosome.
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;
KW Reference proteome.
FT CHAIN 1..539
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063342"
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 477..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 344
FT /note="V -> I (in Ref. 1; CAA44697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 57367 MW; E649BC7D2D14EE29 CRC64;
MAKTLLFGEE ARRSMQAGVD KLANTVKVTL GPKGRNVILD KKFGSPLITN DGVTIAREIE
LEDAYENMGA QLVKEVATKT NDVAGDGTTT ATLLAQAIIR EGLKNVTAGA NPILIRNGIK
TAVEKAVEEI QKISKPVNGK EDIARVAAIS AADEKIGKLI ADAMEKVGNE GVITVEESKS
MGTELDVVEG MQFDRGYVSA YMVTDTEKME AVLDNPLVLI TDKKISNIQD LLPLLEQIVQ
AGKKLLIIAD DIEGEAMTTL VVNKLRGTFT CVGVKAPGFG DRRKEMLQDI ATLTGGVVIS
DEVGGDLKEA TLDMLGEAES VKVTKESTTI VNGRGNSEEI KNRVNQIKLQ LEATTSEFDK
EKLQERLAKL AGGVAVVKVG AATETELKES KLRIEDALAA TKAAVEEGIV PGGGTAYVNV
INEVAKLTSD IQDEQVGINI IVRSLEEPMR QIAHNAGLEG SVIIEKVKNS DAGVGFDALR
GEYKDMIKAG IVDPTKVTRS ALQNAASVAS TFLTTEAAVA DIPEKEMPQG AGMGMDGMY
