ID   CH605_BRADU             Reviewed;         541 AA.
AC   Q89LB1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Chaperonin GroEL 5 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 5 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 5 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 5 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL5 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL5 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=blr4635;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000040; BAC49900.1; -; Genomic_DNA.
DR   RefSeq; NP_771275.1; NC_004463.1.
DR   RefSeq; WP_011087406.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89LB1; -.
DR   SMR; Q89LB1; -.
DR   STRING; 224911.27352899; -.
DR   EnsemblBacteria; BAC49900; BAC49900; BAC49900.
DR   GeneID; 64024387; -.
DR   KEGG; bja:blr4635; -.
DR   PATRIC; fig|224911.44.peg.4446; -.
DR   eggNOG; COG0459; Bacteria.
DR   HOGENOM; CLU_016503_3_0_5; -.
DR   InParanoid; Q89LB1; -.
DR   OMA; IVCNDGV; -.
DR   PhylomeDB; Q89LB1; -.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..541
FT                   /note="Chaperonin GroEL 5"
FT                   /id="PRO_0000063298"
FT   BINDING         30..33
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   541 AA;  57017 MW;  F30E1C805E26C4EB CRC64;
     MAHKQVLFHS AAREKILRGA SLLADAVRVT LGPKSKSVLI QKGWGAPIVC NDGVTIAKEF
     DLKDAEENLG AQVLRQLAEK TGDVVGDGTS TSTILAHAIL SDGVRNVVAG ASAIDLKRGL
     DRGTQAAIAA LRAMATPVKS RAEKVQVATI SAHNDASIGE LVADAIEKVG GDGVISVEES
     KTTETLLDVV EGMKFDRGFL SPYFITDADR MESVLQDPYV LLCDHKIGAL RDLVPLLEQV
     AKSGQPLLII AEDIEGEALA TLIVNQLRGV LKACAVKAPG FGDRRKAMLE DIAILTGAQV
     ISEEIGLNLE NATLQQLGRA ARVVADKENT TLIGSGGDRT RIDARLGQIR VEIEKTTSDY
     DREKLEERLA KLSGGVAVIR VGAPTEAEMK AKKEALDDAI SSTKAAVAEG IVPGGGLALL
     RAVAAVAKEE AACEGDERTG VQILRRALEA PARQIAENSA ADGGVVVARM LEGEGSIGFD
     ASRKVYVDLV AAGIVDPVKV VRTALENAVS VASVLLLTEA TMTEIPEPKR ERLPEPDLAV
     Q