CH60_SYNE7
ID CH60_SYNE7 Reviewed; 544 AA.
AC P22879; Q31KS6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
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=cpn60, groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
GN OrderedLocusNames=Synpcc7942_2313;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1975581; DOI=10.1128/jb.172.9.5079-5088.1990;
RA Webb R., Reddy K.J., Sherman L.A.;
RT "Regulation and sequence of the Synechococcus sp. strain PCC 7942 groESL
RT operon, encoding a cyanobacterial chaperonin.";
RL J. Bacteriol. 172:5079-5088(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; M58751; AAA27314.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58343.1; -; Genomic_DNA.
DR PIR; B36721; BVYCGL.
DR RefSeq; WP_011244099.1; NC_007604.1.
DR AlphaFoldDB; P22879; -.
DR SMR; P22879; -.
DR STRING; 1140.Synpcc7942_2313; -.
DR PRIDE; P22879; -.
DR EnsemblBacteria; ABB58343; ABB58343; Synpcc7942_2313.
DR KEGG; syf:Synpcc7942_2313; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_3; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2313-MON; -.
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; 2.
DR SUPFAM; SSF52029; SSF52029; 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..544
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063569"
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 305..306
FT /note="GL -> AR (in Ref. 1; AAA27314)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="P -> R (in Ref. 1; AAA27314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 57980 MW; 75CF9DDF02B194B9 CRC64;
MAKRIIYNEN ARRALEKGID ILAEAVAVTL GPKGRNVVLE KKFGAPQIIN DGVTIAKEIE
LEDHIENTGV ALIRQAASKT NDAAGDGTTT ATVLAHAVVK EGLRNVAAGA NAILLKRGID
KATNFLVEQI KSHARPVEDS KSIAQVGAIS AGNDFEVGQM IADAMDKVGK EGVISLEEGK
SMTTELEVTE GMRFDKGYIS PYFATDTERM EAVFDEPFIL ITDKKIGLVQ DLVPVLEQVA
RAGRPLVIIA EDIEKEALAT LVVNRLRGVL NVAAVKAPGF GDRRKAMLED IAVLTGGQLI
TEDAGLKLDT TKLDQLGKAR RITITKDNTT IVAEGNEAAV KARVDQIRRQ IEETESSYDK
EKLQERLAKL SGGVAVVKVG AATETEMKDR KLRLEDAINA TKAAVEEGIV PGGGTTLAHL
APQLEEWATA NLSGEELTGA QIVARALTAP LKRIAENAGL NGAVISERVK ELPFDEGYDA
SNNQFVNMFT AGIVDPAKVT RSALQNAASI AAMVLTTECI VVDKPEPKEK APAGAGGGMG
DFDY
