CH60_BUCAP
ID CH60_BUCAP Reviewed; 548 AA.
AC Q59177; Q93A25;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 130.
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, symL;
GN OrderedLocusNames=BUsg_019;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Anwarul H.K., Moriya S., Baumann P., Yoshikawa H., Ogasawara N.;
RT "The nucleotide sequence of 60K, tdhF, groES and groEL genes of Buchnera
RT aphidicola.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9516544; DOI=10.1007/pl00006760;
RA Clark M.A., Baumann L., Baumann P.;
RT "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera
RT aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon,
RT gidA, and rho.";
RL Curr. Microbiol. 36:158-163(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wu Y., Lin L., Cui X.;
RT "Schizaphis graminum endosymbiont GroEL-related molecular chaperonin SymL
RT (symL) gene.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC38099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA12847.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D85628; BAA12847.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF008210; AAC38099.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF434719; AAL30419.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67591.1; -; Genomic_DNA.
DR RefSeq; WP_011053557.1; NC_004061.1.
DR AlphaFoldDB; Q59177; -.
DR SMR; Q59177; -.
DR STRING; 198804.BUsg_019; -.
DR PRIDE; Q59177; -.
DR EnsemblBacteria; AAM67591; AAM67591; BUsg_019.
DR KEGG; bas:BUsg_019; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_6; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000000416; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT CHAIN 1..548
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063306"
FT REGION 526..548
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 479..481
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 2
FT /note="G -> A (in Ref. 3; AAL30419)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..187
FT /note="TGLQNEL -> QVFKNER (in Ref. 3; AAL30419)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="S -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 57851 MW; 0007B98E93CA3491 CRC64;
MGAKDVKFGN EARIKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPSIT KDGVSVAREI
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATLLAQSIV NEGLKAVAAG MNPMDLKRGI
DKAVISAVEE LKNLSVPCSD SKAITQVGTI SANADEKVGA LIAEAMEKVG NDGVITVEEG
TGLQNELEVV KGMQFDRGYL SPYFINKPET GIVELENPYI LMADKKISNV REMLPILESV
AKSGKPLLII SEDLEGEALA TLVVNSMRGI VKVAAVKAPG FGDRRKAMLQ DISILTGGSV
ISEELAMDLE KSTLEDLGQA KRVVINKDTT TIIGGSGEKQ AIQSRIGQIR QEIQEATSDY
DKEKLNERLA KLSGGVAVLK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALV
RVAGKISNLR GHNEDQNVGI RVALRAMEAP LRQIVSNSGE EPSVVTNNVK DGKGNYGYNA
ATDEYGDMID FGILDPTKVT RSALQYAASV AGLMITTECM VTDLPREDKS SDVASSPAGG
MGGMGGMM
