CH60_PARDE
ID CH60_PARDE Reviewed; 545 AA.
AC Q9Z462;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, 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}, mopA;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yohda M., Sumi M., Yoshida M., Fukami T.A., Miki K.;
RT "Molecular cloning and sequencing of chaperonin from Paracoccus
RT denitrificans.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), AND SUBUNIT.
RX PubMed=11563912; DOI=10.1006/jmbi.2001.4961;
RA Fukami T.A., Yohda M., Taguchi H., Yoshida M., Miki K.;
RT "Crystal structure of chaperonin-60 from Paracoccus denitrificans.";
RL J. Mol. Biol. 312:501-509(2001).
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, ECO:0000269|PubMed:11563912}.
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; AB015985; BAA36516.2; -; Genomic_DNA.
DR RefSeq; WP_011749890.1; NZ_PPGA01000014.1.
DR PDB; 1IOK; X-ray; 3.20 A; A/B/C/D/E/F/G=1-545.
DR PDBsum; 1IOK; -.
DR AlphaFoldDB; Q9Z462; -.
DR SMR; Q9Z462; -.
DR PRIDE; Q9Z462; -.
DR OMA; TDTDKME; -.
DR EvolutionaryTrace; Q9Z462; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Isomerase;
KW Nucleotide-binding.
FT CHAIN 1..545
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063469"
FT REGION 526..545
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 STRAND 4..8
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 88..108
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 113..132
FT /evidence="ECO:0007829|PDB:1IOK"
FT TURN 141..145
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:1IOK"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 317..325
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 386..409
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:1IOK"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 423..427
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 434..446
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 449..458
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:1IOK"
FT TURN 481..484
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:1IOK"
FT HELIX 498..516
FT /evidence="ECO:0007829|PDB:1IOK"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:1IOK"
SQ SEQUENCE 545 AA; 57721 MW; 463916AF78335566 CRC64;
MAAKEVKFNS DARDRMLKGV NILADAVKVT LGPKGRNVVI DKSFGAPRIT KDGVSVAKEI
ELSDKFENMG AQMVREVASR TNDEAGDGTT TATVLAQAIV REGLKAVAAG MNPMDLKRGI
DVATAKVVEA IKSAARPVND SSEVAQVGTI SANGESFIGQ QIAEAMQRVG NEGVITVEEN
KGMETEVEVV EGMQFDRGYL SPYFVTNADK MIAELEDAYI LLHEKKLSSL QPMVPLLESV
IQSQKPLLIV AEDVEGEALA TLVVNKLRGG LKIAAVKAPG FGDRRKAMLQ DIAILTGGQV
ISEDLGMKLE NVTIDMLGRA KKVSINKDNT TIVDGAGEKA EIEARVSQIR QQIEETTSDY
DREKLQERVA KLAGGVAVIR VGGMTEIEVK ERKDRVDDAL NATRAAVQEG IVVGGGVALV
QGAKVLEGLS GANSDQDAGI AIIRRALEAP MRQIAENAGV DGAVVAGKVR ESSDKAFGFN
AQTEEYGDMF KFGVIDPAKV VRTALEDAAS VAGLLITTEA MIAEKPEPKA PAGGMPDMGG
MGGMM
