CH606_BRADU
ID CH606_BRADU Reviewed; 546 AA.
AC Q89IK8;
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 6 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 6 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 6 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 6 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL6 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL6 {ECO:0000255|HAMAP-Rule:MF_00600};
GN OrderedLocusNames=blr5626;
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; BAC50891.1; -; Genomic_DNA.
DR RefSeq; NP_772266.1; NC_004463.1.
DR RefSeq; WP_011088372.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89IK8; -.
DR SMR; Q89IK8; -.
DR STRING; 224911.27353902; -.
DR EnsemblBacteria; BAC50891; BAC50891; BAC50891.
DR GeneID; 64025392; -.
DR KEGG; bja:blr5626; -.
DR PATRIC; fig|224911.44.peg.5549; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR InParanoid; Q89IK8; -.
DR OMA; PYILINQ; -.
DR PhylomeDB; Q89IK8; -.
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..546
FT /note="Chaperonin GroEL 6"
FT /id="PRO_0000063299"
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 546 AA; 57751 MW; 98AE98D394B92309 CRC64;
MAAKEVKFSV DARDKMLRGV DILANAVKVT LGPKGRNVVL DKSFGAPRIT KDGVTVAKEI
ELEDKFENMG AQMVREVASK SADAAGDGTT TATVLAQAIV REGAKSVAAG MNPMDLKRGI
DLAVEAVVAD LVKNSKKVTS NDEIAQVGTI SANGDAEIGK FLADAMKKVG NEGVITVEEA
KSLETELDVV EGMQFDRGYI SPYFVTNADK MRVEMDDAYI LINEKKLSSL NELLPLLEAV
VQTGKPLVIV AEDVEGEALA TLVVNRLRGG LKVAAVKAPG FGDRRKAMLQ DIAILTGGQA
ISEDLGIKLE NVTLNMLGRA KKVMIDKENT TIVNGAGKKA DIEARVSQIK AQIEETTSDY
DREKLQERLA KLAGGVAVIR VGGATEVEVK ERKDRVDDAM HATRAAVEEG IVPGGGVALL
RASEQLKGLR TKNDDQKTGV EIVRKALSAP ARQIAINAGE DGSVIVGKIL ENKTYAYGFD
SQTGEYVNLV TKGIIDPTKV VRTAIQNAAS VAALLITTEA MVAELPKKGG AGPAMPPGGG
MGGMDF
