CH607_BRADU
ID CH607_BRADU Reviewed; 543 AA.
AC Q89DA6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Chaperonin GroEL 7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 7 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL7 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL7 {ECO:0000255|HAMAP-Rule:MF_00600};
GN OrderedLocusNames=blr7533;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC52798.1; -; Genomic_DNA.
DR RefSeq; NP_774173.1; NC_004463.1.
DR RefSeq; WP_011090265.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89DA6; -.
DR SMR; Q89DA6; -.
DR STRING; 224911.27355816; -.
DR EnsemblBacteria; BAC52798; BAC52798; BAC52798.
DR GeneID; 64027289; -.
DR KEGG; bja:blr7533; -.
DR PATRIC; fig|224911.44.peg.7636; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR InParanoid; Q89DA6; -.
DR OMA; TDTDKME; -.
DR PhylomeDB; Q89DA6; -.
DR Proteomes; UP000002526; 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; 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;
KW Reference proteome.
FT CHAIN 1..543
FT /note="Chaperonin GroEL 7"
FT /id="PRO_0000063300"
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"
SQ SEQUENCE 543 AA; 57249 MW; B10CFF728A76811D CRC64;
MAAKDVKFSG DARERMLRGV DILANAVKVT LGPKGRNVVI EKSFGAPRIT KDGVTVAKEI
ELEDKFENMG AQMVREVASK TNDLAGDGTT TATVLAQAIV REGAKAVAAG MNPMDLKRGI
DIAVAAVIKD IEKRAKPVAS SSEVAQVGTI SANGDAAIGK MIAQAMQKVG NEGVITVEEN
KSLDTEVDIV EGMKFDRGYL SPYFVTNAEK MTAELEDAYI LLHEKKLSGL QAMLPVLEAV
VQSGKPLVII AEDVEGEALA TLVVNRLRGG LKVAAVKAPG FGDRRKAMLE DLAILTGGQL
ISEELGIKLE NVTVKMLGRA KKVVIDKENT TIVNGAGKKP DIEARVGQIK AQIEETTSDY
DREKLQERLA KLAGGVAVIR VGGATEIEVK EKKDRVEDAL NATRAAVQEG IVPGGGVALL
RAKKAVGRLT NANDDVQAGI NIVLKALEAP IRQISENAGV EGSIVVGKIL ENKSETFGFD
AQNEDYVDMV EKGIIDPAKV VRTALQDASS VAGLLVTTEA MVAEAPKKDA PPAMPAGGGM
GGF
