CH60_ALKHC
ID CH60_ALKHC Reviewed; 544 AA.
AC O50305; Q9KFC3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=BH0562;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=8987660; DOI=10.1271/bbb.60.1633;
RA Xu Y., Kobayashi T., Kudo T.;
RT "Molecular cloning and nucleotide sequence of the groEL gene from the
RT alkaliphilic Bacillus sp. strain C-125 and reactivation of thermally
RT inactivated alpha-glucosidase by recombinant GroEL.";
RL Biosci. Biotechnol. Biochem. 60:1633-1636(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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 -!- INDUCTION: By heat shock.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D55630; BAA09494.1; -; Genomic_DNA.
DR EMBL; BA000004; BAB04281.1; -; Genomic_DNA.
DR PIR; B83720; B83720.
DR PIR; JC5130; JC5130.
DR RefSeq; WP_010896739.1; NC_002570.2.
DR AlphaFoldDB; O50305; -.
DR SMR; O50305; -.
DR STRING; 272558.10173175; -.
DR EnsemblBacteria; BAB04281; BAB04281; BAB04281.
DR KEGG; bha:BH0562; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_9; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000001258; 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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063273"
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"
FT CONFLICT 407
FT /note="E -> VK (in Ref. 1; BAA09494)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="Missing (in Ref. 1; BAA09494)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="A -> VP (in Ref. 1; BAA09494)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="Missing (in Ref. 1; BAA09494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 57404 MW; C769ED81C903C971 CRC64;
MAKDIKFSED ARRSMLRGVD KLADAVKVTL GPKGRNVVLE KKFGSPLITN DGVTIAKEIE
LEDAFENMGA KLVAEVASKT NDIAGDGTTT ATVLAQAMIR EGLKNVTSGA NPMVIRKGIE
KATQVAVEEL SKISKPIEGK DSIAQVAAIS SADDEVGKII AEAMERVGND GVITIEESKG
FSTELEVVEG MQFDRGYASP YMVTDSDKME AVLDNPYVLI TDKKISNIQE VLPVLEQVVQ
QGKPILIIAE DVEGEALATL VVNKLRGTFN AVAVKAPGFG DRRKAMLEDI AILTGGEVIT
EDLGLDLKSA NITQLGRASK VVVTKENTTI VEGAGESDKI AARVNQIKAQ IEETTSDFDK
EKLQERLAKL AGGVAVLKVG AATETEMKER KLRIEDALNS TRAAVEEGIV AGGGTALVNV
IKAVSSIGAE GDEATGVNIV LRALEEPVRQ IAHNAGLEGS VIVERLKKEE AGFGFNAATG
EWVNMVEAGI VDPTKVTRSA LQHAASVSAM FLTTEAVIAD KPEENEGGGG MPDMGGMGGM
GGMM
