CH60_HELPY
ID CH60_HELPY Reviewed; 546 AA.
AC P42383;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, 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}, hsp60, hspB, mopA;
GN OrderedLocusNames=HP_0010;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=8105364; DOI=10.1111/j.1365-2958.1993.tb01724.x;
RA Macchia G., Massone A., Burroni D., Covacci A., Censini S., Rappuoli R.;
RT "The Hsp60 protein of Helicobacter pylori: structure and immune response in
RT patients with gastroduodenal diseases.";
RL Mol. Microbiol. 9:645-652(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=85P;
RX PubMed=7715457; DOI=10.1111/j.1365-2958.1994.tb01331.x;
RA Suerbaum S., Thiberge J.-M., Kansau I., Ferrero R.L., Labigne A.;
RT "Helicobacter pylori hspA-hspB heat-shock gene cluster: nucleotide
RT sequence, expression, putative function and immunogenicity.";
RL Mol. Microbiol. 14:959-974(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X73840; CAA52062.1; -; Genomic_DNA.
DR EMBL; L23798; AAC41441.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07080.1; -; Genomic_DNA.
DR PIR; B64521; S36237.
DR RefSeq; NP_206812.1; NC_000915.1.
DR RefSeq; WP_001040293.1; NC_018939.1.
DR AlphaFoldDB; P42383; -.
DR SMR; P42383; -.
DR DIP; DIP-3069N; -.
DR IntAct; P42383; 11.
DR MINT; P42383; -.
DR STRING; 85962.C694_00045; -.
DR PaxDb; P42383; -.
DR EnsemblBacteria; AAD07080; AAD07080; HP_0010.
DR KEGG; hpy:HP_0010; -.
DR PATRIC; fig|85962.47.peg.9; -.
DR eggNOG; COG0459; Bacteria.
DR OMA; TDTDKME; -.
DR PhylomeDB; P42383; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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; Stress response.
FT CHAIN 1..546
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063389"
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 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT VARIANT 76
FT /note="V -> D (in strain: 85P)"
FT VARIANT 123
FT /note="A -> P (in strain: 85P)"
FT VARIANT 293
FT /note="I -> V (in strain: 85P)"
FT VARIANT 320..321
FT /note="GR -> K (in strain: 85P)"
FT CONFLICT 339
FT /note="H -> D (in Ref. 1; CAA52062)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="A -> T (in Ref. 1; CAA52062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 58264 MW; 00E5DB7FAAC82282 CRC64;
MAKEIKFSDS ARNLLFEGVR QLHDAVKVTM GPRGRNVLIQ KSYGAPSITK DGVSVAKEIE
LSCPVANMGA QLVKEVASKT ADAAGDGTTT ATVLAYSIFK EGLRNITAGA NPIEVKRGMD
KAAEAIINEL KKASKKVGGK EEITQVATIS ANSDHNIGKL IADAMEKVGK DGVITVEEAK
GIEDELDVVE GMQFDRGYLS PYFVTNAEKM TAQLDNAYIL LTDKKISSMK DILPLLEKTM
KEGKPLLIIA EDIEGEALTT LVVNKLRGVL NIAAVKAPGF GDRRKEMLKD IAILTGGQVI
SEELGLSLEN AEVEFLGKAG RIVIDKDNTT IVDGKGHSHD VKDRVAQIKT QIASTTSDYD
KEKLQERLAK LSGGVAVIKV GAASEVEMKE KKDRVDDALS ATKAAVEEGI VIGGGAALIR
AAQKVHLNLH DDEKVGYEII MRAIKAPLAQ IAINAGYDGG VVVNEVEKHE GHFGFNASNG
KYVDMFKEGI IDPLKVERIA LQNAVSVSSL LLTTEATVHE IKEEKAAPAM PDMGGMGGMG
GMGGMM
