CH60_BRECH
ID CH60_BRECH Reviewed; 543 AA.
AC Q8RU00;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Brevibacillus choshinensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HPD31;
RX PubMed=11471738; DOI=10.1271/bbb.65.1379;
RA Tokunaga M., Shiraishi Y., Odachi M., Mizukami M., Tokunaga H., Philo J.S.,
RA Arakawa T., Ishibashi M., Tanaka R., Takagi H.;
RT "Molecular cloning of groESL locus, and purification and characterization
RT of chaperonins, GroEL and GroES, from Bacillus brevis.";
RL Biosci. Biotechnol. Biochem. 65:1379-1387(2001).
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; AB038650; BAB85116.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RU00; -.
DR SMR; Q8RU00; -.
DR STRING; 54911.AN963_28435; -.
DR PRIDE; Q8RU00; -.
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.
FT CHAIN 1..543
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063301"
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 543 AA; 57383 MW; ED526D92F90C9545 CRC64;
MAKQVKFSED APRSMLRGVE TLPNAVKVTL GPKGRNVVLE KKFGSPLITN DGVTIPKEIE
LEDAYENMGA QLVKEVATKT NGIAGDGTTT ATVLAAAMIR EGLKNVAAGA NPMVIRRGME
KAVGAAVEEI KSIAKPVENK SSIAQVAAIS ADDQEVGNLI AEAMEKVGKD GVITVEESKG
FVTELEVVEG MQFDRGYASP YMITDTDKME AVLNNPFILI TDKKISNIQE VLPVLEQVVQ
SGKPLLIIAE DVEGEALATL VVNKLRGTFT AVAVKAPGFG DRRKAMLQDI AALTGGEVIT
EELGLDLKST KLEQLGRAGK IVVTKENTTV VEGAGDKANI ESRVAQIRQQ IEDTTSDFDR
EKLQERLAKL AGGVAVIKVG AATETELKEK KLRIEDALNS TRAAVEEGIV PGGGTTLINA
IKAVEGVKVE GEEAVGVHIV LRSLEEPVRQ IAANAGLEGS VIVERLKKEP VGIGFNAATE
EYVNMLEAGI VDAAKVTRSA LSNAASVAAM FLTTEAVIAD KPEENKAPMG MPDMGGMGGM
GMM
