CH60_HAEDU
ID CH60_HAEDU Reviewed; 547 AA.
AC P31294;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 09-SEP-2003, sequence version 2.
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;
GN OrderedLocusNames=HD_1784;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1356926; DOI=10.1128/iai.60.10.4111-4118.1992;
RA Parsons L.M., Waring A.L., Shayegani M.;
RT "Molecular analysis of the Haemophilus ducreyi groE heat shock operon.";
RL Infect. Immun. 60:4111-4118(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; M91030; AAA24961.1; -; Genomic_DNA.
DR EMBL; AE017143; AAP96536.1; -; Genomic_DNA.
DR PIR; B49203; B49203.
DR AlphaFoldDB; P31294; -.
DR SMR; P31294; -.
DR STRING; 233412.HD_1784; -.
DR MoonProt; P31294; -.
DR EnsemblBacteria; AAP96536; AAP96536; HD_1784.
DR KEGG; hdu:HD_1784; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_6; -.
DR Proteomes; UP000001022; 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..547
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063386"
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 37
FT /note="N -> K (in Ref. 1; AAA24961)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="A -> V (in Ref. 2; AAP96536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 57798 MW; B9DF933AD998B5C8 CRC64;
MAIKDVKFGN DARVKMLKGV NILADAVKVT LGPKGRNVVL DKAYGAPTIT KDGVSVAREI
ELEDKFENMG AQMVKEVASK ANDVAGDGTT TATVLAQSIV SEGLRAVAAG MNPMDLKRGI
DKAVAAVVEE LKAISKPCET SKEIEQVGTI SANSDETVGK LIAQAMEKVG KEGVITVEDG
TGLDDALDVV EGMQFDRGYL SPYFINKPEA GTVELDNPYI ILVDKKISNI REILPVLEAV
AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIAILTAGTV
ISEEIGMELE KATLEELGQA KRVVITKDNT TIIDGIGDEA QIKARVVQIR QQIEDSTSDY
DKEKLQERVA KLAGGVAVIK VGAATEVAMK EKKDRVDDAL HATRAAVEEG IVPGGGVALV
RAANKVSATL TGDNEEQNVG IKLALRAMEA PLRQIVENSG EDASVVARDV KDGSGNFGYN
ATTEEYGDML EMGILDPTKV TRSALQFAAS IAGLMITTEC MITDLPKEDK LDAQAAMGGM
GGMGGMM
