CH60_CAMJE
ID CH60_CAMJE Reviewed; 545 AA.
AC O69289; Q0P935; Q9PN75;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 131.
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;
GN OrderedLocusNames=Cj1221;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10206714; DOI=10.1099/13500872-145-1-89;
RA Thies F.L., Weishaupt A., Karch H., Hartung H.P., Giegerich G.;
RT "Cloning, sequencing and molecular analysis of the Campylobacter jejuni
RT groESL bicistronic operon.";
RL Microbiology 145:89-98(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43429 / MK5-S7630 / Serotype O:1,
RC ATCC 43432 / MK7 / Serotype O:4, ATCC 43438 / MK1 / Serotype O:10, and
RC ATCC 43456 / MK290 / Serotype O:36;
RA Cunningham A., Taboada E., Nash J.H., Wakarchuk W.W., Gilbert M.;
RT "Sequencing of the cpn60 gene from various Campylobacter jejuni isolates.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; Y13334; CAA73778.1; -; Genomic_DNA.
DR EMBL; AF461064; AAL76936.1; -; Genomic_DNA.
DR EMBL; AF461534; AAL67841.1; -; Genomic_DNA.
DR EMBL; AF461535; AAL67842.1; -; Genomic_DNA.
DR EMBL; AF461537; AAL67844.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL35336.1; -; Genomic_DNA.
DR PIR; G81328; G81328.
DR RefSeq; WP_002858047.1; NC_002163.1.
DR RefSeq; YP_002344612.1; NC_002163.1.
DR AlphaFoldDB; O69289; -.
DR SMR; O69289; -.
DR IntAct; O69289; 96.
DR STRING; 192222.Cj1221; -.
DR PaxDb; O69289; -.
DR PRIDE; O69289; -.
DR EnsemblBacteria; CAL35336; CAL35336; Cj1221.
DR GeneID; 905511; -.
DR KEGG; cje:Cj1221; -.
DR PATRIC; fig|192222.6.peg.1203; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_7; -.
DR OMA; TDTDKME; -.
DR Proteomes; UP000000799; 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; 2.
DR SUPFAM; SSF52029; SSF52029; 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..545
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063322"
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 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 477..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 179
FT /note="A -> P (in Ref. 1; CAA73778)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="A -> T (in Ref. 1; CAA73778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 57971 MW; 4DA80BC64330C41E CRC64;
MAKEIIFSDE ARNKLYEGVK KLNDAVKVTM GPRGRNVLIQ KSFGAPSITK DGVSVAKEVE
LKDSLENMGA SLVREVASKT ADQAGDGTTT ATVLAHAIFK EGLRNITAGA NPIEVKRGMD
KACEAIVAEL KKLSREVKDK KEIAQVATIS ANSDEKIGNL IADAMEKVGK DGVITVEEAK
SINDELNVVE GMQFDRGYLS PYFITNAEKM TVELSSPYIL LFDKKITNLK DLLPVLEQIQ
KTGKPLLIIA EDIEGEALAT LVVNKLRGVL NISAVKAPGF GDRRKAMLED IAILTGGEVI
SEELGRTLES ATIQDLGQAS SVIIDKDNTT IVNGAGEKAN IDARVNQIKA QIAETTSDYD
REKLQERLAK LSGGVAVIKV GAATETEMKE KKDRVDDALS ATKAAVEEGI VIGGGAALIK
AKAKIKLDLQ GDEAIGAAIV ERALRAPLRQ IAENAGFDAG VVVNSVENAK DENTGFDAAK
GEYVNMLESG IIDPVKVERV ALLNAVSVAS MLLTTEATIS EIKEDKPTMP DMSGMGGMGG
MGGMM
