ID CH604_BRADU Reviewed; 543 AA.
AC Q89P00;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Chaperonin GroEL 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 4 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groEL, groL4 {ECO:0000255|HAMAP-Rule:MF_00600};
GN OrderedLocusNames=blr3683;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; 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, ECO:0000305}.
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DR EMBL; BA000040; BAC48948.1; -; Genomic_DNA.
DR RefSeq; NP_770323.1; NC_004463.1.
DR RefSeq; WP_011086464.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89P00; -.
DR SMR; Q89P00; -.
DR STRING; 224911.AAV28_15415; -.
DR EnsemblBacteria; BAC48948; BAC48948; BAC48948.
DR GeneID; 64023415; -.
DR KEGG; bja:blr3683; -.
DR PATRIC; fig|224911.44.peg.3347; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_5; -.
DR InParanoid; Q89P00; -.
DR OrthoDB; 9766614at2; -.
DR PhylomeDB; Q89P00; -.
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: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; 3.50.7.10; GroEL; 1.
DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 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 4"
FT /id="PRO_0000063297"
FT BINDING 29..32
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 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 476..478
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"
SQ SEQUENCE 543 AA; 56659 MW; 555F36077A6C5574 CRC64;
MPKVLLHDIE ARRALARGVQ KLAAAIESTL GPKGMNAMVD RPIGTPIVSR DGVTIASEIE
LPDRFENMGA QVVREVSMQT NEVAGDGTTT AMVLANGLIQ GGVAALERGA KAVDLCKGID
RAVEVVVESL KSAAIPVSDR RTLQAVATIA STDSHLGDLI AEAVERVGKD GIISSDYGLT
TSTTLEVVEG MSFDRGYISH HMVTDVEKME VVLEQPYILL TDLKIKAPGE LAAVRARVAE
TGKPLVIVAE EIAPEVVVTL LGEGNRGKVL VVNPPDYGHW RKAMMDDLAI ITGGRVIARE
LGGMLEEASL ADLGTARQVR ASARETVIIR GGGDDAAIAA RRQQVAKQHD LAPPNIEQDK
LKERLAKLSG GTAVIFAGGV TPVEQKRTIQ LIDDALSAAR AAAEEGIVPG GGTALAQCAP
VVVRALGNIN GDLGEGIKLV RETLSRPAAF IARNAGHDAA KVVAELQSSR AGVGFDAANG
VFIDMVSAGI VDPVRVTYTA LRNAASVATL VLTTNTLVAD VPEYVDPTQG PALGGGAEKL
GRA
//
