CH60_YEREN
ID CH60_YEREN Reviewed; 550 AA.
AC P48219;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
DE AltName: Full=Cross-reacting protein antigen;
DE AltName: Full=Heat shock protein 60;
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=crpA, groL {ECO:0000255|HAMAP-Rule:MF_00600}, hsp60, mopA;
OS Yersinia enterocolitica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Y-108C / Serotype O:3;
RA Haefner C.E., Roggenkamp A.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WA / Serotype O:8;
RA Autenrieth I.B., Noll A.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype O:3;
RX PubMed=8190995; DOI=10.1016/0923-2508(93)90033-x;
RA Yamamoto T., Miura H., Ohsumi K., Yamaguchi H., Taguchi H., Ogata S.;
RT "Cloning and nucleotide sequence analysis of immunodominant heat-shock
RT protein of Yersinia enterocolitica.";
RL Res. Microbiol. 144:691-701(1993).
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; X68526; CAA48539.1; -; Genomic_DNA.
DR EMBL; X82212; CAA57694.1; -; Genomic_DNA.
DR EMBL; D14078; BAA03164.1; -; Genomic_DNA.
DR PIR; S26423; S26423.
DR PIR; S52901; S52901.
DR AlphaFoldDB; P48219; -.
DR SMR; P48219; -.
DR STRING; 1443113.LC20_04829; -.
DR eggNOG; COG0459; Bacteria.
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 Stress response.
FT CHAIN 1..550
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063614"
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 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT VARIANT 2
FT /note="A -> P (in strain: WA / Serotype O:8)"
FT VARIANT 355
FT /note="E -> D (in strain: WA / Serotype O:8)"
FT CONFLICT 16..17
FT /note="ML -> IV (in Ref. 3; BAA03164)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="S -> Y (in Ref. 1; CAA48539)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> P (in Ref. 1; CAA48539)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="A -> V (in Ref. 1; CAA48539)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="V -> L (in Ref. 3; BAA03164)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="A -> T (in Ref. 1; CAA48539)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="H -> D (in Ref. 3; BAA03164)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="A -> R (in Ref. 3; BAA03164)"
FT /evidence="ECO:0000305"
FT CONFLICT 473..482
FT /note="AGSGSYGYNA -> RVQVATVTS (in Ref. 3; BAA03164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 57527 MW; 2269A4B18E39DA4F CRC64;
MAAKDVKFGN DARIKMLRGV NILADAVKVT LGPKGRNVVL DKSFGSPTIT KDGVSVAREI
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQSII TEGLKAVAAG MNPMDLKRGI
DKAVIAAVEE LKKLSVPCSD SKAIAQVGTI SANSDSTVGE LIAQAMEKVG KEGVITVEEG
SGLQDELDVV EGMQFDRGYL SPYFINKPET GSIELESPFI LLADKKISNI REMLPVLEAV
AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTAGTV
ISEEIGLELE KTTLEDLGQA KRVVINKDTT IIIDGVGDEA AIQGRVAQIR QQIEEATSDY
DKEKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI
RAASAITAAG LKGDNEDQNV GIKVALRAME SPLRQIVVNA GEEASVIANN VKAGSGSYGY
NAYSEEYGDM IAMGILDPTK VTRSALQYAA SIAGLMITTE CMITDLPRDD KGADMGAGGM
GGMGGMGGMM
