CH60_WOLPP
ID CH60_WOLPP Reviewed; 552 AA.
AC B3CL71;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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}; OrderedLocusNames=WP0027;
OS Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=570417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wPip;
RX PubMed=18550617; DOI=10.1093/molbev/msn133;
RA Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL Mol. Biol. Evol. 25:1877-1887(2008).
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; AM999887; CAQ54136.1; -; Genomic_DNA.
DR RefSeq; WP_007302814.1; NC_010981.1.
DR AlphaFoldDB; B3CL71; -.
DR SMR; B3CL71; -.
DR STRING; 570417.WP0027; -.
DR PRIDE; B3CL71; -.
DR EnsemblBacteria; CAQ54136; CAQ54136; WP0027.
DR KEGG; wpi:WP0027; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR Proteomes; UP000008814; 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..552
FT /note="Chaperonin GroEL"
FT /id="PRO_1000130077"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 50
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 420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 552 AA; 58983 MW; E1CB4DDADD510F24 CRC64;
MANIVVSGEQ LQEAFREVAA MVDSTVGATA GPRGNTIGIS KPYGGPEVTK DGYKVMKGIK
PEKPLHSAIV STIAQSASQC NDKVGDGTTT CSILTSNMIM EASKSIAAGN DRICIKNGIQ
KAKDVILKEI TSMSRTISLE KMDEVAQVAI ISANGDKDIG NSIADAVKKV GKEGVITVEE
SKGSKELEVE LTTGMQFDRG YLSPYFVTNN EKMSVELDDP YLLITEKKLN IIQPLLPILE
AIFKSGKPLF IIAEDVEGEA LSTLVINKLR GLKVAAVKAP GFGDRRKEML EDIAALTGAK
YVIKDELGIK MEDLTLEDLG TAKNVKITKD NTTIVSEDSD CDKQNRVNAR INQIKSQIET
STSDYDKEKL RERLAKLSGG VAVLKVGGAT EVEVKERRDR VEDALHATRA AIEEGIVPGG
GVALLYAASA LDKLKASSDE EQIGINIVKK VLSAPIKRLV KNAGLESAVI IDYLIKQNDK
ELIYNVEAMN YANASTAGVI DPAKVVRIAF ETAVSVASAL ITTESMIVDL PNKEENASSP
MGAGAMGGMG GF
