CH60_ACEP3
ID CH60_ACEP3 Reviewed; 546 AA.
AC Q8GBD2; C7JC84;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 97.
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=APA01_17870;
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01;
RX PubMed=16233284; DOI=10.1263/jbb.94.140;
RA Okamoto-Kainuma A., Yan W., Kadono S., Tayama K., Koizumi Y., Yanagida F.;
RT "Cloning and characterization of groESL operon in Acetobacter aceti.";
RL J. Biosci. Bioeng. 94:140-147(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01;
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
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; AB081586; BAC16232.1; -; Genomic_DNA.
DR EMBL; AP011121; BAH99912.1; -; Genomic_DNA.
DR RefSeq; WP_003625762.1; NC_013209.1.
DR AlphaFoldDB; Q8GBD2; -.
DR SMR; Q8GBD2; -.
DR STRING; 634452.APA01_17870; -.
DR PRIDE; Q8GBD2; -.
DR EnsemblBacteria; BAH99912; BAH99912; APA01_17870.
DR GeneID; 60376731; -.
DR GeneID; 66351959; -.
DR KEGG; apt:APA01_17870; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; TDTDKME; -.
DR BioCyc; APAS634452:APA01_RS09055-MON; -.
DR Proteomes; UP000000948; 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;
KW Reference proteome.
FT CHAIN 1..546
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063250"
FT REGION 527..546
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"
FT CONFLICT 17..18
FT /note="LR -> RA (in Ref. 1; BAC16232)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="KA -> NV (in Ref. 1; BAC16232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 58135 MW; F5DCCEE0521A65C1 CRC64;
MAAKDVKFGA DARQRMLRGV DILADAVKVT LGPKGRNVVL DKSFGAPRIT KDGVSVAKEI
ELADKFENMG AQMLREVASK TNDIAGDGTT TATVLAQAIV REGHKAVAAG MNPMDLKRGI
DKAVAVVIEE LKKNAKKVTT PAETAQVGTI SANGESEIGQ MISEAMQKVG SEGVITVEEA
KHFQTELDVV EGMQFDRGYI SPYFVTNPEK MTADLENPYI LIHEKKLSSL QPMLPLLESV
VQSGRPLLII AEDVDGEALA TLVVNKLRGG LKIAAVKAPG FGDRRKAMLE DIAILTGGQV
ISEDLGIKLE TVTLNMLGTA KKVHIDKENT TIVDGAGKAD DIKGRVKQIR AQIEETSSDY
DREKLQERLA KLAGGVAVIR VGGSTEVEVK ERKDRVDDAL HATRAAVEEG IVPGGGTALA
RATLKLEGLH YHNDDQRVGG DIIRRALQAP LRQIAHNAGE DGAVIANKVL ENSDYNFGFD
AQAGEYKNLV EAGIIDPAKV VRTALQDAAS VAGLLITTEA MVAERPEKKA APAGGPDMGG
MGGMDF
