CH60_CHLPM
ID CH60_CHLPM Reviewed; 547 AA.
AC A4SDP9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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};
GN OrderedLocusNames=Cvib_0586;
OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS vibrioformis (strain DSM 265)).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 265 / 1930;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA Schuster S.C., Bryant D.A., Richardson P.;
RT "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL Submitted (MAR-2007) 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; CP000607; ABP36608.1; -; Genomic_DNA.
DR RefSeq; WP_011889836.1; NC_009337.1.
DR AlphaFoldDB; A4SDP9; -.
DR SMR; A4SDP9; -.
DR STRING; 290318.Cvib_0586; -.
DR PRIDE; A4SDP9; -.
DR EnsemblBacteria; ABP36608; ABP36608; Cvib_0586.
DR KEGG; pvi:Cvib_0586; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_10; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
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..547
FT /note="Chaperonin GroEL"
FT /id="PRO_1000082483"
FT REGION 527..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 87..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 547 AA; 58252 MW; B8F1990AE682490A CRC64;
MTAKDILFDA DARAKLKVGV DKLANAVKVT LGPAGRNVLI DKKFGAPTST KDGVTVAKEV
ELEDAIENMG AQMVREVASK TSDVAGDGTT TATVLAQAIY REGLKNVAAG ARPIDLKRGI
DRAVKEVVAE LRTISRSISG KKEIAQVGTI SANNDPEIGE LIAEAMDKVG KDGVITVEEA
KGMDTELKVV EGMQFDRGYL SPYFVTNSES MEAELDDALI LIYDKKISNM KELLPILEKG
AQSGRPLLII AEDIEGEALA TLVVNKLRGT LKVCAVKAPG FGDRRKAMLD DIAILTGGTV
ISEEKGYKLE NATINYLGQA ARVSLDKDNT TIVEGKGTQE EIKARINEIK GQIDKSTSDY
DTEKLQERLA KLSGGVAVLN IGASTEVEMK EKKARVEDAL HATRAAVQEG IVVGGGVALI
RAIKGLDNAK PDNDDQKTGI EIIRRALEEP LRQIVANTGT TDGAVVLEHV KNGEGDYGFN
ARTEQYENLV EAGVVDPTKV TRSALENAAS VASILLTTEA CITDIKENTP DMPAMPPGGM
GGMGGMY
